This document discusses post-translational modifications (PTMs), which are enzymatic modifications of proteins after translation. It describes various types of PTMs like trimming, covalent attachments through phosphorylation, glycosylation, sulfation, methylation, and hydroxylation. The importance of PTMs in regulating protein function and cellular processes is highlighted. Detection methods for PTMs like mass spectrometry and fluorescent staining are also mentioned.
Reverse transcription of RNA, which refers to the conversion of the RNA template into its complimentary DNA strand (cDNA) is an essential step in the analysis of gene transcripts.
cDNA can be sequenced, cloned and applied to estimate the copy number of specific genes in order to characterize and to validate gene expression.
Reverse transcription of RNA, which refers to the conversion of the RNA template into its complimentary DNA strand (cDNA) is an essential step in the analysis of gene transcripts.
cDNA can be sequenced, cloned and applied to estimate the copy number of specific genes in order to characterize and to validate gene expression.
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
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Post translation control-regulation_of_gene_expression_in_eukaryotes - copyDhruviSuvagiya
Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins following protein biosynthesis. Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product. PTMs are important components in cell signaling, as for example when prohormones are converted to hormones.
This presentation explores a brief idea about the structural and functional attributes of nucleotides, the structure and function of genetic materials along with the impact of UV rays and pH upon them.
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Nutraceutical market, scope and growth: Herbal drug technologyLokesh Patil
As consumer awareness of health and wellness rises, the nutraceutical market—which includes goods like functional meals, drinks, and dietary supplements that provide health advantages beyond basic nutrition—is growing significantly. As healthcare expenses rise, the population ages, and people want natural and preventative health solutions more and more, this industry is increasing quickly. Further driving market expansion are product formulation innovations and the use of cutting-edge technology for customized nutrition. With its worldwide reach, the nutraceutical industry is expected to keep growing and provide significant chances for research and investment in a number of categories, including vitamins, minerals, probiotics, and herbal supplements.
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
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Richard's entangled aventures in wonderlandRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Slide 1: Title Slide
Extrachromosomal Inheritance
Slide 2: Introduction to Extrachromosomal Inheritance
Definition: Extrachromosomal inheritance refers to the transmission of genetic material that is not found within the nucleus.
Key Components: Involves genes located in mitochondria, chloroplasts, and plasmids.
Slide 3: Mitochondrial Inheritance
Mitochondria: Organelles responsible for energy production.
Mitochondrial DNA (mtDNA): Circular DNA molecule found in mitochondria.
Inheritance Pattern: Maternally inherited, meaning it is passed from mothers to all their offspring.
Diseases: Examples include Leber’s hereditary optic neuropathy (LHON) and mitochondrial myopathy.
Slide 4: Chloroplast Inheritance
Chloroplasts: Organelles responsible for photosynthesis in plants.
Chloroplast DNA (cpDNA): Circular DNA molecule found in chloroplasts.
Inheritance Pattern: Often maternally inherited in most plants, but can vary in some species.
Examples: Variegation in plants, where leaf color patterns are determined by chloroplast DNA.
Slide 5: Plasmid Inheritance
Plasmids: Small, circular DNA molecules found in bacteria and some eukaryotes.
Features: Can carry antibiotic resistance genes and can be transferred between cells through processes like conjugation.
Significance: Important in biotechnology for gene cloning and genetic engineering.
Slide 6: Mechanisms of Extrachromosomal Inheritance
Non-Mendelian Patterns: Do not follow Mendel’s laws of inheritance.
Cytoplasmic Segregation: During cell division, organelles like mitochondria and chloroplasts are randomly distributed to daughter cells.
Heteroplasmy: Presence of more than one type of organellar genome within a cell, leading to variation in expression.
Slide 7: Examples of Extrachromosomal Inheritance
Four O’clock Plant (Mirabilis jalapa): Shows variegated leaves due to different cpDNA in leaf cells.
Petite Mutants in Yeast: Result from mutations in mitochondrial DNA affecting respiration.
Slide 8: Importance of Extrachromosomal Inheritance
Evolution: Provides insight into the evolution of eukaryotic cells.
Medicine: Understanding mitochondrial inheritance helps in diagnosing and treating mitochondrial diseases.
Agriculture: Chloroplast inheritance can be used in plant breeding and genetic modification.
Slide 9: Recent Research and Advances
Gene Editing: Techniques like CRISPR-Cas9 are being used to edit mitochondrial and chloroplast DNA.
Therapies: Development of mitochondrial replacement therapy (MRT) for preventing mitochondrial diseases.
Slide 10: Conclusion
Summary: Extrachromosomal inheritance involves the transmission of genetic material outside the nucleus and plays a crucial role in genetics, medicine, and biotechnology.
Future Directions: Continued research and technological advancements hold promise for new treatments and applications.
Slide 11: Questions and Discussion
Invite Audience: Open the floor for any questions or further discussion on the topic.
Comparing Evolved Extractive Text Summary Scores of Bidirectional Encoder Rep...University of Maribor
Slides from:
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Track: Artificial Intelligence
https://www.etran.rs/2024/en/home-english/
2. Contents:
What is Translation?
Components Of Translation.
PTMs
Trimming
Covalent Attachments
Protein Folding
Protein Degaradation
Detection of PTMs
Importance of PTMs
Disorders related to PTMs
Conclusion
3. Post Translational Modifications can be defined
as:
Covalent or generally enzymatic modifications
of proteins during or after the synthesis of the proteins.
Before understanding about it, first of all we must have
information about the Translation.
4. Translation:
In Molecular Biology Translation refers to the
formation of proteins from mRNA with the help of the
ribosomes present in the cytoplasm of the cell in the
case of prokaryotes while in eukaryotes translation is
carried out at the membrane pf RER or in the cytosol.
The mRNA decoded from DNA is migrated into the
cytoplasm for the synthesis of proteins that then fold,
acquire a tertiary conformation and perform their
perspective functions.
5. Components required for Translation:
Amino Acids
tRNA
mRNA
Functionally components Ribosomes
Protein Factors
ATP and GTP required as energy sources.
8. Types Of Post Translational Modifications:
Post translational modifications or PTMs are involved in
modifying the protein structure after they have been
translated according to information on the mRNA.
The post translational modifiactions can
be enzymatic or covalent.
In the human body these PTMs increases the diversity
and accuracy of proteins.
9. Types Of PTMs:
PTMs can be catagorized as:
Trimming
Cavalent Attachments
Protein Folding
Protein Degradation
10. Trimming:
Insuline is synthesized in the cells and it is
in inactive form that it is can’t perform it’s function. For
the proper functioning of insuline its post translational
modifications occurs that have involve the removal of
the part of protein to convert it into a three
dimensional and fully active form
12. Covalent Attachments:
Covalent attachments refers to the addition or the
transfer of the polypeptide chain that acts as an
acceptor region. In this way, proteins are modified for
the diversity of function.it includes:
Phosphorylation
Glycosylation
Sulfation
Methylation
Hydroxylation
13. Phosphorylation:
Phosphoryalation is the addition of one or
more phosphate groups to the protein. Post
Translational Phosphorylation is one of the most
common protein modifications that occur in animal
cells. The vast majorirtis of phosphorylation occur as a
mechanism to regulate the biological activity of a
protein and as such are transient.
In animal cells Serine, tyrosine and thereonine are the
amino acids that subjected to the phosphorylation.
15. Glycosylation:
Glycosylation is the addition of carbohydrate molecules
to the polypeptide chain and modifying it into
glycoproteins. Many of the proteins that are destined to
become a part of plasma membrane or to be secreted
from the cell, have carbohydrate chains attached to the
amide nitrogen of asparagine(N linked) or the hydroxyl
groups of serine, threonine(O linked). N glycosylation
occurs in ER and O glycosylation occurs in the Golgi
Complex.
17. Sulfation:
Sulfate modidication takes place by the addition of
sulphate molecules and these modifications of proteins
occurs at tyrosine residues.Tyrosine sulfation
accomplished via the activity of
tyrosylproteinsulfotransferases (TPST) which are
membrane associated enzymes of trans-Golgi network.
There are two known TPSTs.
TPST-1
TPST-2
The universal phosphate donor is 3’-phosphoadenosyl-
5’-phosphosulphate (PSPA).
19. Methylation:
The transfer of one-carbon methyl groups to nitrogen
or oxygen to amino acid side chains increases the
hydrophobicity of the protein and can neutralize a
negative amino acid charge when bound to carboxylic
acids. Methylation is mediated by methyltransferases
and S-adenosyl methionine (SAM) is the primary
methyl group donor.
21. Hydroxylation:
The biological process of addition of a hydroxy group
to a protein amino acid is called Hydroxylation. Protein
hydroxylation is one type of PTM that involves the
conversion of –CH group into –COH group and these
hydroxylated amino acids are involved in the regulation
of some important factors called transcription factors.
Among 20, the two amino acids can be regulated these
are proline and lysine.
23. Other covalent Modifications:
Some other covalent
modifications of the polypeptide chains involve the following
processes.
Carboxylation
Lipidation
Biotinylation
Acetylation
25. Protein Degradation:
Proteins that are defective for example, misfolded or
destined for rapid turnover are often marked for
destruction by ubi ubiquitination-the attachment of
chains of a small, highly conserved protein, called
ubiquitin. Proteins marked in this way are rapidly
degraded by a cellular component known as the
proteasome, which is a macromolecular, ATP-
dependent, proteolytic system located in the cytosol.
26. Proteins must fold to assume
their functional state. Folding can be spontaneous
or facilitated by proteins known as Cheperones.
Protein Folding:
27. Detection of PTM:
There are several chemical and biological techniques
for the detection of PTMs that whether the
modification has occurred or completed in the protein
or not. These methods are very helpful and advanced
now a day for in vitro use too. The methods are:
•Mass Spectrometry
•Florescent staining of two dimensional gels
•Immune system activation
•By affinity binding DNA
28. There are some of the pictures that had shown the detection of
post translational modifications of proteins by different methods.
Fig: showing detection of PTM by 2D page imaging:
30. Importance Of PTMs:
Post translational modifications are very important for the cells
to live and progress. Some of the points related to the
importance of the PTMs are listed below as:
•Post-translational modifications of proteins, which are not gene-
template based, can regulate the protein functions, by causing
changes in protein activity, their cellular locations and dynamic
interactions with other proteins.
•Acetylation regulates many diverse functions, including DNA
recognition, protein-protein interaction and protein stability
•Redox-dependent PTM of proteins is emerging as a key signaling
system conserved through evolution, influences many aspects of
cellular homeostasis
31. •Protein lipid-modifications including myristoylation,
palmitoylation, farnesylation, and prenylation, known for a long
time, have been shown to have a role in protein-membrane
interactions, protein trafficking, and enzyme activity.
It is also evident that glycosylation plays a key role in immune
regulation, e.g. in the development, survival and reactivity of T
cells