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1. Translation
SUBMITTED BY --- SAHIL VERMA
SUBMITTED TO --– DR. JYOTI GULERIA
CLASS. --- MSC 2ND SEM.
(MAJOR ZOOLOGY)
UNV. ROLL. ---- 81232730028

2. Translation
Definition : - The synthesis of protein from mRNA
involves translation of the language of nucleic acids
into language of proteins.

3. TRANSLATION IN PROKARYOTES
The cellular machinery involved in translation are :-
 Ribosome - Ribosomes are macromolecular machines that direct the synthesis of proteins.
And play crucial role in orienting the mRNA and amino acid- carrying tRNAs in such a
manner that the genetic code can be read accurately.

4. . tRNA molecules :-
 tRNA molecules serve as adaptors, enabling sequence
of codons in mRNA to ultimately determine the amino
acid sequence of polypeptide chain.
 Transfer RNA plays a vital role as an intermediary
between mRNA and amino acids.
H

6.  The name of the amino acid that attaches to given tRNA is indicated by superscript. For example,
tRNA molecules specific for amino acid alanine are designated as tRNAAla. After attachment, the
tRNA is now called an aminoacyl tRNA (e.g., alanyl tRNAAla). The tRNA is now said to be in its
charged form, and the amino acid is said to be activated.
 • Each tRNA possesses an anticodon, which is a special trinucleotide sequence located within one
of the loops of the tRNA molecule. The tRNA molecules can recognize codons in mRNA .The
anticodon of each tRNA are complementary to one or more mRNA codons that specify the amino
acid being carried by that tRNA. The codons in mRNA are represented in the 5ˊ → 3ˊ direction,
whereas anticodons in tRNA are usually written in the 3ˊ → 5ˊ orientation. Thus, if one of the
codons for alanine is 5ˊ –GCC -3ˊ, the corresponding anticodon in tRNA

7. Aminoacyl-tRNA Synthetases :-
 A minoacyl –tRNA synthetases are the enzymes responsible for linking amino
acids to their correspondin tRNAs.

8. mRNA template:-
 The genetic information is encoded onto mRNA which acts as a template for
polypeptide synthesis. Prokaryotes have polycistronic mRNAs with multiple
translation start site.

9. Factors involved in Prokaryotic
translation:-

10. Steps involved in Translation :-
Charging of tRNA:-

11. Initiation

12. Elongation
Three stages of Polypeptide Chain Elongation in Bacteria :-
 1. An aminoacyl tRNA binds to the A site with the help of GTP-bound EF-Tu. During binding of
tRNA, GTP gets hydrolyzed and EF-Tu is released. The recycling is supported by EF-Tu.
 2. A peptide bond is formed at the P site between the –COOH group of fMet (and COOH of
terminal amino acid in later cycles) and the newly arrived amino acid at the A-site.
 3. The mRNA advances by three nucleotides. The peptidyl tRNA moves from the A site to the P
site. Also the empty tRNA moves from the P site to the E site. During the process, GTP bound to
EF-G gets hydrolysed

14. Termination
 Elongation process continues, reading one codon after another and adding successive amino acids in polypeptide chain, until any one of the
three chain-termination (stop) codons (UAG, UAA, or UGA) in the mRNA arriveLs.
 enters the ribosome’s A site. Since there are no tRNAs with anticodons complementary to the termination codon, no tRNA enters the A site
of the ribosome when a termination codon is encountered. Instead, the stop codons are recognized by proteins called release factors which
possess special regions (‘peptide anticodons’) that bind to mRNA stop codons present at ribosomal A site. E. Coli has three release factors –
RF1, RF2 and RF3. Release factor1 recognizes and binds to the termination codons UAA and UAG, while RF2 binds to UGA and UAA. The
binding of RF1 or RF2 to the A site of the ribosome promotes the cleavage of the tRNA in the P site from the polypeptide chain and the
release of polypeptide. The release factor 3 binds to the ribosome and forms a complex with GTP. This binding brings about conformational
change in the ribosome, releasing RF1 or RF2 from the A site and causing the tRNA in the P site to move to the E site. In this process GTP is
hydrolyzed to GDP. Additional factors help bring about the release of the tRNA from the P site, the release of the mRNA .
 enters the ribosome’s A site. Since there are no tRNAs with anticodons complementary to the termination codon, no tRNA enters the A site
of the ribosome when a termination codon is encountered. Instead, the stop codons are recognized by proteins called release factors which
possess special regions (‘peptide anticodons’) that bind to mRNA stop codons present at ribosomal A site. E. Coli has three release factors –
RF1, RF2 and RF3. Release factor1 recognizes and binds to the termination codons UAA and UAG, while RF2 binds to UGA and UAA. The
binding of RF1 or RF2 to the A site of the ribosome promotes the cleavage of the tRNA in the P site from the polypeptide chain and the
release of polypeptide. The release factor 3 binds to the ribosome and forms a complex with GTP. This binding brings about conformational
change in the ribosome, releasing RF1 or RF2 from the A site and causing the tRNA in the P site to move to the E site. In this process GTP is
hydrolyzed to GDP (Figure 13.11). Additional factors help bring about the release of the tRNA from the P site, the release of the mRNA from
the

16. References:-
 Google.com./YouTube. Com.
 Byjus the learning app.
 IGNOU Notes
 Cell &Molecular biology by Wilson & Walker.