Translation is the process by which the genetic code stored in mRNA is used to synthesize proteins. It involves mRNA being read by ribosomes, which link amino acids in the order specified by the mRNA codons. There are four main steps: 1) activation of amino acids, 2) initiation by forming the initiation complex on the mRNA start codon, 3) elongation where the growing polypeptide chain is extended, 4) termination when a stop codon is reached and the protein is released. The fidelity of translation is ensured by tRNAs, ribosomes, and various translation factors.
This document discusses protein synthesis (translation) including:
1. The components required for translation such as amino acids, tRNA, mRNA, ribosomes.
2. The main steps of translation - activation, initiation, elongation, termination, and post-translational modification.
3. Differences between prokaryotic and eukaryotic translation processes.
4. How various drugs can inhibit protein synthesis or nucleic acid synthesis to treat bacterial infections or cancer.
1. Translation is the process by which the genetic code stored in mRNA is used to direct the assembly of proteins from amino acids using ribosomes and tRNAs.
2. Initiation involves the assembly of the ribosome and initiation factors at the start codon on the mRNA. Elongation then adds amino acids one by one to the growing polypeptide chain through the actions of elongation factors.
3. Termination occurs when a stop codon is reached, releasing the completed protein and dissociating the ribosome into its subunits. The protein may then undergo further processing to become functional.
INTRODUCTION
HISTORY
MECHANISM OF PROTEIN SYNTHESIS
TRANSCRIPTION
TRANSLATION
TRANSCRIPTION
INITIATION
ELONGATION
TERMINATION
TRANSLATION
AMINOACYLATION OF tRNA
INITIATION OF POLYPEPTIDE CHAIN
ELONGATION
TERMINATION
CONCLUSION
REFERENCES
Introduction.
History.
Central dogma.
Mechanism of protein synthesis.
Transcription.
Process of transcription
translation
Step of translation
Activation of amino acid.
Transfer of amino acid to tRNA.
Initiation of polypeptide chain
Elongation of polypeptide chain
Translocation
Termination of polypeptide chain
processing of released polypeptide chain
Main difference between protein synthesis in prokaryotes and eukryotes
Conclusion
Reference
This document summarizes the process of translation. Translation is the process by which the sequence of nucleotides in messenger RNA directs the incorporation of amino acids into a protein. It involves three main steps - initiation, elongation, and termination. Initiation requires various initiation factors and ribosomal subunits to form the initiation complex. Elongation is a cyclic process of aminoacyl-tRNA binding, peptide bond formation, and translocation. Termination occurs when a stop codon is reached, releasing the polypeptide chain. Ribosomal recycling then dissociates the post-termination complex to prepare the ribosome for another round of translation.
Translation is the process by which messenger RNA (mRNA) is used to produce proteins. It involves decoding the mRNA to build a polypeptide chain of amino acids. Translation requires several components, including amino acids, ribosomes, mRNA, transfer RNA (tRNA), and protein factors. It occurs through three main stages - initiation, elongation, and termination. Initiation involves assembling the ribosome and first tRNA on the mRNA start codon. Elongation is the process of linking amino acids together via peptide bonds. Termination occurs when a stop codon is reached, releasing the complete protein chain. The new protein may then undergo further processing and modification.
Protein synthesis in eukaryotes involves three main steps - initiation, elongation, and termination. Initiation requires many initiation factors and begins with formation of a preinitiation complex on the 5' end of mRNA. Elongation is cyclic and adds one amino acid at a time to the growing polypeptide chain using elongation factors. Termination occurs when a stop codon is reached and release factors cause dissociation of the ribosome and polypeptide release. Additional processes like post-translational modifications further process the final protein structure and function.
It is the process of synthesis of protein by encoding information on mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and enzyme aminoacyl tRNA synthase
This document discusses protein synthesis (translation) including:
1. The components required for translation such as amino acids, tRNA, mRNA, ribosomes.
2. The main steps of translation - activation, initiation, elongation, termination, and post-translational modification.
3. Differences between prokaryotic and eukaryotic translation processes.
4. How various drugs can inhibit protein synthesis or nucleic acid synthesis to treat bacterial infections or cancer.
1. Translation is the process by which the genetic code stored in mRNA is used to direct the assembly of proteins from amino acids using ribosomes and tRNAs.
2. Initiation involves the assembly of the ribosome and initiation factors at the start codon on the mRNA. Elongation then adds amino acids one by one to the growing polypeptide chain through the actions of elongation factors.
3. Termination occurs when a stop codon is reached, releasing the completed protein and dissociating the ribosome into its subunits. The protein may then undergo further processing to become functional.
INTRODUCTION
HISTORY
MECHANISM OF PROTEIN SYNTHESIS
TRANSCRIPTION
TRANSLATION
TRANSCRIPTION
INITIATION
ELONGATION
TERMINATION
TRANSLATION
AMINOACYLATION OF tRNA
INITIATION OF POLYPEPTIDE CHAIN
ELONGATION
TERMINATION
CONCLUSION
REFERENCES
Introduction.
History.
Central dogma.
Mechanism of protein synthesis.
Transcription.
Process of transcription
translation
Step of translation
Activation of amino acid.
Transfer of amino acid to tRNA.
Initiation of polypeptide chain
Elongation of polypeptide chain
Translocation
Termination of polypeptide chain
processing of released polypeptide chain
Main difference between protein synthesis in prokaryotes and eukryotes
Conclusion
Reference
This document summarizes the process of translation. Translation is the process by which the sequence of nucleotides in messenger RNA directs the incorporation of amino acids into a protein. It involves three main steps - initiation, elongation, and termination. Initiation requires various initiation factors and ribosomal subunits to form the initiation complex. Elongation is a cyclic process of aminoacyl-tRNA binding, peptide bond formation, and translocation. Termination occurs when a stop codon is reached, releasing the polypeptide chain. Ribosomal recycling then dissociates the post-termination complex to prepare the ribosome for another round of translation.
Translation is the process by which messenger RNA (mRNA) is used to produce proteins. It involves decoding the mRNA to build a polypeptide chain of amino acids. Translation requires several components, including amino acids, ribosomes, mRNA, transfer RNA (tRNA), and protein factors. It occurs through three main stages - initiation, elongation, and termination. Initiation involves assembling the ribosome and first tRNA on the mRNA start codon. Elongation is the process of linking amino acids together via peptide bonds. Termination occurs when a stop codon is reached, releasing the complete protein chain. The new protein may then undergo further processing and modification.
Protein synthesis in eukaryotes involves three main steps - initiation, elongation, and termination. Initiation requires many initiation factors and begins with formation of a preinitiation complex on the 5' end of mRNA. Elongation is cyclic and adds one amino acid at a time to the growing polypeptide chain using elongation factors. Termination occurs when a stop codon is reached and release factors cause dissociation of the ribosome and polypeptide release. Additional processes like post-translational modifications further process the final protein structure and function.
It is the process of synthesis of protein by encoding information on mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and enzyme aminoacyl tRNA synthase
This document summarizes key aspects of protein synthesis, including translation of mRNA into a polypeptide chain. It discusses the genetic code and how triplet codons specify amino acids. The stages of translation - initiation, elongation, and termination - are described. Post-translational modifications and protein degradation are also covered. Protein synthesis requires various ribosomal and transfer RNA components to translate the genetic message into proteins.
Ribosomes translate mRNA into polypeptides. They consist of two subunits containing rRNA and proteins. tRNAs carry specific amino acids and recognize mRNA codons through complementary base pairing between their anticodons. Translation involves initiation, elongation, and termination. During initiation, the small ribosomal subunit binds the 5' end of mRNA. Elongation adds amino acids to the growing polypeptide chain through peptide bond formation. Termination releases the polypeptide when a stop codon is reached. Accurate protein synthesis depends on specific interactions between mRNA codons, tRNA anticodons, and the ribosomal subunits.
L6, Translation and genetic code_17a7ea13763061b9ec93113a467b074d.pdfjrdys25ycm
Erythromycin helps Ali by inhibiting the process of translation in Streptococcus pneumonia bacteria. During translation, erythromycin binds to the 50S ribosomal subunit and prevents the translocation step. This stops the synthesis of bacterial proteins and kills the bacteria causing Ali's pneumonia infection.
Translation is the process by which the genetic code carried by mRNA is used to synthesize proteins. It requires ribosomes, tRNA, amino acids, and various enzymes. There are three main steps: initiation begins protein synthesis using initiator tRNA; elongation joins amino acids through peptide bond formation and translocation; and termination releases the complete polypeptide when a stop codon is reached. The newly formed protein then undergoes post-translational modifications to achieve its functional structure and may combine with other proteins. Multiple ribosomes can translate the same mRNA simultaneously as a polysome.
Translation in eukaryotes involves three main steps - initiation, elongation, and termination. Initiation begins with the dissociation of ribosomes into subunits, followed by the formation of initiation complexes involving initiation factors and met-tRNA binding to the 40S subunit. Elongation cyclicly adds amino acids to the growing polypeptide chain through aminoacyl-tRNA binding, peptide bond formation, and translocation. Termination occurs when a release factor binds to a stop codon, causing the ribosomal subunits to separate and release the completed polypeptide chain. Ribosomal recycling then dissociates remaining mRNA and tRNAs to recycle the ribosome.
The document summarizes protein biosynthesis and inhibition. It describes how protein biosynthesis requires mRNA, tRNA, ribosomes, amino acids and other factors. The key steps are activation of amino acids by attaching them to tRNA, and protein synthesis on ribosomes via initiation, elongation and termination. Several antibiotics inhibit protein synthesis by targeting different steps like initiation, elongation or translocation. Streptomycin causes misreading, tetracycline blocks tRNA binding, and chloramphenicol inhibits peptidyltransferase.
Ribosomes translate mRNA messages into proteins through the process of translation. Translation involves three main steps - initiation, elongation, and termination. In initiation, the small ribosomal subunit binds to the 5' end of mRNA and scans for the start codon. In elongation, amino acids are sequentially added to the growing polypeptide chain through the formation of peptide bonds. Termination occurs when a stop codon is reached, causing the ribosome to dissociate and release the completed protein. Transfer RNA molecules (tRNAs) play a key role by carrying amino acids and matching them to mRNA codons through complementary base pairing of their anticodons. Enzymes like peptidyl transferase catalyze bond formation. The overall process
The document provides information about protein synthesis and processing. It begins with an overview of the topics to be covered, including ribosome formation, initiation and elongation factors, termination, the genetic code, tRNA aminoacylation, aminoacyl-tRNA synthetases, translational proofreading, inhibitors, and post-translational modifications. It then discusses the machinery of protein synthesis, including transcription, the genetic code, RNA, tRNA identity, aminoacyl-tRNA synthetases, aminoacylation of tRNA, and the ribosome. The mechanisms of initiation, elongation, and termination are explained in detail.
Translation of mRNA into protein occurs through three main stages: initiation, elongation, and termination. During initiation, the ribosome assembles on the mRNA with the help of initiation factors. In elongation, tRNAs bring amino acids to the ribosome according to the mRNA codons and link them together to form the polypeptide chain. Termination occurs when a stop codon enters the A site, signaling the release of the complete protein. In eukaryotes, post-translational modifications such as phosphorylation, acetylation, and protein folding further process the protein to produce its active form.
Post-transcriptional modifications process the primary transcript RNA in eukaryotic cells through 5' capping, polyadenylation at the 3' end, and splicing of introns. This processing protects the RNA from degradation, aids in export from the nucleus to the cytoplasm, and allows only protein-coding exons to be translated, increasing protein synthesis efficiency. Alternative splicing also expands the proteome by producing multiple mRNA variants from a single primary transcript.
Translation is the process by which the information contained in mRNA is used to synthesize proteins. It occurs in four main phases: initiation, elongation, termination, and recycling. During initiation, the small and large ribosomal subunits assemble around the mRNA. In elongation, tRNAs bring amino acids to the ribosome according to the mRNA sequence, forming peptide bonds. Termination occurs when a stop codon is reached, releasing the complete protein. The ribosomal subunits and other factors are then recycled to translate more mRNA.
Translation is the process of translating the sequence of a messenger RNA (mRNA) molecule to a sequence of amino acids during protein synthesis. The genetic code describes the relationship between the sequence of base pairs in a gene and the corresponding amino acid sequence that it encodes.
27 28 105 fa13 transcription and translation skelAfton Chase
The document summarizes transcription and translation in bacteria and eukaryotes. It describes the central dogma where DNA is transcribed into mRNA which is translated into protein. Transcription involves initiation, elongation, and termination. Translation involves initiator tRNAs bringing amino acids to the ribosome where they are linked together into a polypeptide chain. Eukaryotic transcription and translation are more complex than prokaryotes with mRNA processing and separate transcription/translation.
1. Translation is the process by which the instructions in mRNA are used to synthesize proteins. It involves transcription of DNA to mRNA and then translation of mRNA to protein.
2. During translation, transfer RNA (tRNA) molecules carry amino acids and line up with mRNA codons in ribosomes. Enzymes link the amino acids together to form a polypeptide chain.
3. Translation occurs in three steps - initiation, elongation, and termination. In initiation, the ribosome and first tRNA bind to mRNA. In elongation, amino acids are linked together. In termination, the ribosome releases the full protein.
Gene expression & protein synthesisssuserc4adda
Gene expression involves the transcription of DNA into mRNA and the translation of mRNA into proteins. There are four main stages of protein synthesis: activation, initiation, elongation, and termination. Transcription is regulated by promoters, enhancers, and response elements that control the rate of transcription and influence which genes are expressed. Translation includes quality control mechanisms to ensure accuracy, such as ensuring amino acids are bound to the proper tRNAs and that termination occurs at stop codons. Mutations can occur during DNA replication or transcription and may be caused by mutagens, though cells have repair mechanisms. Recombinant DNA techniques allow genes to be spliced from one organism into a plasmid or virus for protein production in other cells.
Messenger RNA carries genetic code from DNA and is translated by the ribosome into proteins. This involves transfer RNA molecules that associate amino acids with their codons. Translation begins with initiation factors recruiting the small ribosomal subunit to the start codon. Elongation then occurs through peptide bond formation catalyzed by the ribosome and translocation of transfer RNAs. Termination occurs when a stop codon is reached. Translation is highly conserved and essential for protein synthesis in all organisms.
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This document summarizes key aspects of protein synthesis, including translation of mRNA into a polypeptide chain. It discusses the genetic code and how triplet codons specify amino acids. The stages of translation - initiation, elongation, and termination - are described. Post-translational modifications and protein degradation are also covered. Protein synthesis requires various ribosomal and transfer RNA components to translate the genetic message into proteins.
Ribosomes translate mRNA into polypeptides. They consist of two subunits containing rRNA and proteins. tRNAs carry specific amino acids and recognize mRNA codons through complementary base pairing between their anticodons. Translation involves initiation, elongation, and termination. During initiation, the small ribosomal subunit binds the 5' end of mRNA. Elongation adds amino acids to the growing polypeptide chain through peptide bond formation. Termination releases the polypeptide when a stop codon is reached. Accurate protein synthesis depends on specific interactions between mRNA codons, tRNA anticodons, and the ribosomal subunits.
L6, Translation and genetic code_17a7ea13763061b9ec93113a467b074d.pdfjrdys25ycm
Erythromycin helps Ali by inhibiting the process of translation in Streptococcus pneumonia bacteria. During translation, erythromycin binds to the 50S ribosomal subunit and prevents the translocation step. This stops the synthesis of bacterial proteins and kills the bacteria causing Ali's pneumonia infection.
Translation is the process by which the genetic code carried by mRNA is used to synthesize proteins. It requires ribosomes, tRNA, amino acids, and various enzymes. There are three main steps: initiation begins protein synthesis using initiator tRNA; elongation joins amino acids through peptide bond formation and translocation; and termination releases the complete polypeptide when a stop codon is reached. The newly formed protein then undergoes post-translational modifications to achieve its functional structure and may combine with other proteins. Multiple ribosomes can translate the same mRNA simultaneously as a polysome.
Translation in eukaryotes involves three main steps - initiation, elongation, and termination. Initiation begins with the dissociation of ribosomes into subunits, followed by the formation of initiation complexes involving initiation factors and met-tRNA binding to the 40S subunit. Elongation cyclicly adds amino acids to the growing polypeptide chain through aminoacyl-tRNA binding, peptide bond formation, and translocation. Termination occurs when a release factor binds to a stop codon, causing the ribosomal subunits to separate and release the completed polypeptide chain. Ribosomal recycling then dissociates remaining mRNA and tRNAs to recycle the ribosome.
The document summarizes protein biosynthesis and inhibition. It describes how protein biosynthesis requires mRNA, tRNA, ribosomes, amino acids and other factors. The key steps are activation of amino acids by attaching them to tRNA, and protein synthesis on ribosomes via initiation, elongation and termination. Several antibiotics inhibit protein synthesis by targeting different steps like initiation, elongation or translocation. Streptomycin causes misreading, tetracycline blocks tRNA binding, and chloramphenicol inhibits peptidyltransferase.
Ribosomes translate mRNA messages into proteins through the process of translation. Translation involves three main steps - initiation, elongation, and termination. In initiation, the small ribosomal subunit binds to the 5' end of mRNA and scans for the start codon. In elongation, amino acids are sequentially added to the growing polypeptide chain through the formation of peptide bonds. Termination occurs when a stop codon is reached, causing the ribosome to dissociate and release the completed protein. Transfer RNA molecules (tRNAs) play a key role by carrying amino acids and matching them to mRNA codons through complementary base pairing of their anticodons. Enzymes like peptidyl transferase catalyze bond formation. The overall process
The document provides information about protein synthesis and processing. It begins with an overview of the topics to be covered, including ribosome formation, initiation and elongation factors, termination, the genetic code, tRNA aminoacylation, aminoacyl-tRNA synthetases, translational proofreading, inhibitors, and post-translational modifications. It then discusses the machinery of protein synthesis, including transcription, the genetic code, RNA, tRNA identity, aminoacyl-tRNA synthetases, aminoacylation of tRNA, and the ribosome. The mechanisms of initiation, elongation, and termination are explained in detail.
Translation of mRNA into protein occurs through three main stages: initiation, elongation, and termination. During initiation, the ribosome assembles on the mRNA with the help of initiation factors. In elongation, tRNAs bring amino acids to the ribosome according to the mRNA codons and link them together to form the polypeptide chain. Termination occurs when a stop codon enters the A site, signaling the release of the complete protein. In eukaryotes, post-translational modifications such as phosphorylation, acetylation, and protein folding further process the protein to produce its active form.
Post-transcriptional modifications process the primary transcript RNA in eukaryotic cells through 5' capping, polyadenylation at the 3' end, and splicing of introns. This processing protects the RNA from degradation, aids in export from the nucleus to the cytoplasm, and allows only protein-coding exons to be translated, increasing protein synthesis efficiency. Alternative splicing also expands the proteome by producing multiple mRNA variants from a single primary transcript.
Translation is the process by which the information contained in mRNA is used to synthesize proteins. It occurs in four main phases: initiation, elongation, termination, and recycling. During initiation, the small and large ribosomal subunits assemble around the mRNA. In elongation, tRNAs bring amino acids to the ribosome according to the mRNA sequence, forming peptide bonds. Termination occurs when a stop codon is reached, releasing the complete protein. The ribosomal subunits and other factors are then recycled to translate more mRNA.
Translation is the process of translating the sequence of a messenger RNA (mRNA) molecule to a sequence of amino acids during protein synthesis. The genetic code describes the relationship between the sequence of base pairs in a gene and the corresponding amino acid sequence that it encodes.
27 28 105 fa13 transcription and translation skelAfton Chase
The document summarizes transcription and translation in bacteria and eukaryotes. It describes the central dogma where DNA is transcribed into mRNA which is translated into protein. Transcription involves initiation, elongation, and termination. Translation involves initiator tRNAs bringing amino acids to the ribosome where they are linked together into a polypeptide chain. Eukaryotic transcription and translation are more complex than prokaryotes with mRNA processing and separate transcription/translation.
1. Translation is the process by which the instructions in mRNA are used to synthesize proteins. It involves transcription of DNA to mRNA and then translation of mRNA to protein.
2. During translation, transfer RNA (tRNA) molecules carry amino acids and line up with mRNA codons in ribosomes. Enzymes link the amino acids together to form a polypeptide chain.
3. Translation occurs in three steps - initiation, elongation, and termination. In initiation, the ribosome and first tRNA bind to mRNA. In elongation, amino acids are linked together. In termination, the ribosome releases the full protein.
Gene expression & protein synthesisssuserc4adda
Gene expression involves the transcription of DNA into mRNA and the translation of mRNA into proteins. There are four main stages of protein synthesis: activation, initiation, elongation, and termination. Transcription is regulated by promoters, enhancers, and response elements that control the rate of transcription and influence which genes are expressed. Translation includes quality control mechanisms to ensure accuracy, such as ensuring amino acids are bound to the proper tRNAs and that termination occurs at stop codons. Mutations can occur during DNA replication or transcription and may be caused by mutagens, though cells have repair mechanisms. Recombinant DNA techniques allow genes to be spliced from one organism into a plasmid or virus for protein production in other cells.
Messenger RNA carries genetic code from DNA and is translated by the ribosome into proteins. This involves transfer RNA molecules that associate amino acids with their codons. Translation begins with initiation factors recruiting the small ribosomal subunit to the start codon. Elongation then occurs through peptide bond formation catalyzed by the ribosome and translocation of transfer RNAs. Termination occurs when a stop codon is reached. Translation is highly conserved and essential for protein synthesis in all organisms.
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"Market Research it too text-booky, I am in the market for a decade, I am living research book" this is what the founder I met on the event claimed, few of my colleagues rolled their eyes. Its true that one cannot over look the real life experience, but one cannot out beat structured gold mine of market research.
Many 0 to 1 startup founders often overlook market research, but this critical step can make or break a venture, especially in health tech.
But Why do they skip it?
Limited resources—time, money, and manpower—are common culprits.
"In fact, a survey by CB Insights found that 42% of startups fail due to no market need, which is like building a spaceship to Mars only to realise you forgot the fuel."
Sudharsan Srinivasan
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Overconfidence in their product’s success leads founders to assume it will naturally find its market, especially in health tech where patient needs, entire system issues and regulatory requirements are as complex as trying to perform brain surgery with a butter knife. Additionally, the pressure to launch quickly and the belief in their own intuition further contribute to this oversight. Yet, thorough market research in health tech could be the key to transforming a startup's vision into a life-saving reality, instead of a medical mishap waiting to happen.
Example of Market Research working
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Identifying Pain Points: Innovaccer surveyed healthcare providers to understand their difficulties with data integration, care coordination, and patient engagement. They found widespread frustration with siloed systems and inefficient workflows.
Competitive Analysis: Analyzed competitors offering similar solutions in healthcare analytics and interoperability. Identified gaps in comprehensive data aggregation, real-time analytics, and actionable insights.
Regulatory Compliance: Ensured their platform complied with HIPAA and other healthcare data privacy regulations. This compliance was crucial to gaining trust from healthcare providers wary of data security issues.
Customer Validation: Conducted pilot programs with several healthcare organizations to validate the platform's effectiveness in improving care outcomes and operational efficiency. Gathered feedback to refine features and user interface.
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2. Translation
• The translation of the mRNA codons into
amino acid sequences leads to the synthesis
of poypeptides, which then fold and/or
aggregate to form functional molecules called
proteins.
• The word “translation” is well-chosen
because the chemical language of nucleic
acids (in mRNA) is being changed into the
chemical language of polypeptides during the
process.
3. Cont------
• Proteins are the active participants in cell
structure and function.
• They are the “work horses” of the cell
• The main function of the genetic material is,
therefore, to encode the production of cellular
proteins in the correct cell, at the proper time,
and in suitable amounts
• Translation occurs in cytosol on ribosomes
4.
5. Cont------
• Note that the mRNA begins with a 5’
untranslated region
• In other words, the START codon is not at the
5’ end of the mRNA but somewhat
downstream (3’)
• Although it is not shown here, the STOP codon
is likewise not at the 3’ end of the mRNA.
There is a 3’ untranslated region after it.
6. Basic requirements of translation
• mRNA to be translated
• tRNAs (at least 20)
• Ribosomes
• 20 aminoacids
• amino-acyl-tRNAsynthetases (at least 20)
• Energy in the form of ATP and GTP
• Enzymes and protein factors
7. Cont------
mRNA
• It is a template for protein synthesis
• Eukaryotic mRNA is monocystronic meaning
that there is only one coding sequence on
each mRNA producing only one polypeptide
chain
• Prokaryotic mRNA is polycistronic, often
encoding for more than one polypeptide on
the same mRNA.
8. Cont------
tRNA
• It is the adaptor molecule in protein synthesis
• In the 1950s, Francis Crick and Mahon
Hoagland proposed the adaptor hypothesis,
which hypothesized that tRNAs play a direct
role in the recognition of codons in the
mRNA.
• In particular, the hypothesis proposed that
tRNA has two functions:
9. Cont------
1. Recognizing a 3-base codon in mRNA
2. Carrying an amino acid that is specific for
that codon to the translation machinery
• During mRNA-tRNA recognition, the anticodon
in tRNA binds to a complementary codon in
mRNA:
10.
11. Modified Nucleotides and the Wobble
Hypothesis
• In addition to the normal A, U, G and C
nucleotides, tRNAs commonly contain
modified nucleotides
• More than 60 of these can occur
• As mentioned earlier, the genetic code is
degenerate
• With the exception of serine, arginine and
leucine, this degeneracy always occurs at the
codon’s third position
12. Cont------
– To explain this pattern of degeneracy, Francis Crick
proposed in 1966 the wobble hypothesis
– In the codon-anticodon recognition process, the
first two positions pair strictly according to the A –
U /G – C rule
– However, the third position can actually “wobble”
or move a bit, thus tolerating certain types of
mismatches
• The modified nucleotides in the tRNA
anticodon allow this “wobbling” to occur.
13. Cont------
• The anticodon of tRNA identifies a number of
synonym codons of one amino acid that differ
at the 3rd base.
• Examples are the two arginine codons, AGA
and AGG bind same UCU anticodon and the
three glycine codons, GGU, GGC and GGA bind
same CCI anticodon.
14. The Ribosome
• Translation occurs on the surface of a large
macromolecular complex termed the
ribosome
• A ribosome is composed of structures called
the large and small subunits
• Each subunit is formed from the assembly of
• Proteins
• Ribosomal RNA (rRNA)
17. Stages of translation
• The process of protein synthesis includes four
steps:
• I. Activation of amino acids.
• II. Initiation.
• III. Elongation.
• IV. Termination.
18. 1. Activation of amino acids:
• It is catalyzed by amino-acyl-tRNAsynthetase that
is specialized in sticking a specific amino acid to a
specific tRNA, as follows,
• Amino acid + ATP Amino-acyl-AMP + PPi
2Pi
• Amino-acyl-AMP + tRNA Amino-acyl-tRNA +
AMP
• The -COOH of the amino acid binds to the 3'-OH
group of adenine of the acceptor arm of the tRNA
(i.e., 3'-ACC).
19. 2. Initiation:
• Initiation of protein synthesis requires
identification of mRNA for translation by
ribosomes. Requirements of the initiation
step are:
• a) Amino-acyl-tRNA. b) Ribosome. c) mRNA.
d) GTP and ATP.
• e) At least 10 eukaryotic initiation factors
(eIFs).
20. A. Formation of the 40S preinitiation
complex:
• Eukaryotic initiation factor-1 (eIF1) dissociates
the complete ribosome into its 40S and 60S
subunits. Then, initiation factor-3 (eIF-3)
prevents reassociation these subunits.
• The amino-acyl-tRNA (met-tRNA) interacts
with initiation factor-2 (eIF-2) bound to GTP
that enables it to bind the 40S-eIF-1-eIF3
complex to give the 40S preinitiation complex.
21. B. Formation of the 40S initiation
complex:
• Initiation factor-4 (eIF-4) binds the cap of
mRNA and activates it to bind the 40S
preinitiation complex to form the 40S
initiation complex with hydrolysis of ATP into
ADP + Pi.
• This complex scans mRNA for the initiation
AUG that is the 5'-most AUG with a specific
sequence around it.
22. Cont------
• Thus, anticodon of amino-acyl-tRNA is
brought into contact with the translation
initiation codon in mRNA.
• The newly synthesized protein always starts
with methionine (formyl-methionine in
prokaryote) as the N-terminal amino acid as
translation always begins at AUG.
23. C. Formation of the 80S initiation
complex:
• Initiation factor-5 (eIF5) hydrolyzes GTP on eIF2
into GDP + Pi and activates binding of the 40S
initiation complex to 60S ribosomal subunit with
release of initiation factors-1, -2, -3 and -4.
• The complete ribosome contains two amino-acyl-
tRNA-binding sites. These are the P site (peptidyl
site, i.e., preceding amino-acyl-tRNA site carrying
one or more amino acids) and the A site (i.e.,
following amino-acyl-tRNA site).
24. Cont------
• The first amino-acyl-tRNA carrying the first amino
acid in the polypeptide chain will be automatically
located at P site and the next amino-acyl-tRNA
enters at A site, see the figure below.
• When cell is under stress conditions that makes it
unable to synthesize protein, e.g., lake of amino acids
or glucose, growth factor deprivation, or heat shock,
eIF2 undergoes inhibitory phosphorylation by
specific kinases to prevent formation of 40S
preinitiation complex and hence protein synthesis.
25.
26. 3. Elongation:
• An elongation factor-1 (eEF-1) binds with
amino-acyl-tRNA with hydrolysis of GTP into GDP
+ Pi, forming a complex.
• This complex allows amino-acyl-tRNA to enter at
A site of ribosome with the release of eEF-1.
• The free -NH2 group of the new amino acid
binds the -COOH group of the first amino acid
(Met) with the transfer of whole peptide chain to
tRNA at A site by peptidyltransferase with the
release of the free tRNA at P site
27. Cont------
• Elongation factor 2 (eEF-2, translocase) translocates
the whole complex with the newly formed peptidyl-
tRNA a one-codon distance along the mRNA in 5' to
3' direction.
• Translocation requires hydrolysis of GTP into GDP + Pi
and creates a new free A site for entrance of a new
amino-acyl-tRNA to recognize a new codon and so
on.
• Polypeptide chain is thus increased by one amino
acid each time.
28.
29.
30.
31. 4. Termination:
• When a termination codon in mRNA appears
at A-site, there is no tRNA that can recognize
it, but rather, releasing factors (eRFs)
recognize it.
• A releasing factor activates the
peptidyltransferase to hydrolyze and release
the peptide chain on tRNA at P site to free
tRNA then mRNA and 80S ribosome
dissociates into its subunits.
32.
33. Post-translation Modification of
Proteins:
• Activation by hydrolysis of an extra-peptide
(pre-pro-proteins) or zymogens.
• Glycosylation that occurs in endoplasmic
reticulum and Golgi apparatus.
• Hydroxylation of proline and lysine, e.g., in
collagen.
• Phosphorylation of tyrosine, serine or
threonine.
34. Polypeptide Localization
• The amino acid sequences of newly-
synthesized polypeptides contain “sorting
signals” that tell the cell where they belong
• These are especially important in eukaryotes,
where each sorting signal is recognized by a
specific cellular component
• These cellular components facilitate the
sorting of the protein to its correct
compartment
35. Effect of antibiotics on protein
synthesis:
• Many antibiotics selectively inhibit protein
synthesis in bacterial because of the
distinction between eukaryotic and
prokaryotic ribosomal system.
• Aminoglycosides (streptomycin, gentamycin
and amikin), they binds the 30S rRNA and
disturb mRNA binding to the ribosome.
• Tetracyclines prevent the binding of amino-
acyl-tRNA to A site.
36. Cont------
• Chloramphenicol inhibits peptidyltransferase.
• Puromycin has a structure similarity with tyrosyl-
tRNA and cause premature release of the peptide
in both eukaryotes and prokaryotes.
• Cycloheximide inhibits peptidyltransferase in
eukaryotes only.
• Diphtheria exotoxin ADP-ribosylates eEF2 to
inhibit its function.
• Erythromycin Inhibits translocation
37. Cont------
• Many polypeptides will not fold properly and
become functional proteins until they are
properly localized within the cell
• Sometimes, mutations lead to changes in the
amino acid sequence of the polypeptide that
prevent its localization
• Such polypeptides are eventually degraded
• Localization mutations are usually null mutations
(the protein coded by the gene has no residual
function in the cell)