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Peptide chain undergoes folding
Some amino acids might be changed
Carbohydrates or lipids can be added
Peptide can be activated by addition or
removal of some residue (acetate, phosphate,
methyl etc.)
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Changes in the Hydrogen bond tendency
which results in secondary and tertiary
structures
Some of the proteins might remain in cytosol
while others are transported across the
membrane or even imported into cellular
organelles (mitochondria or chloroplasts) to
accomplish their functions
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The chemical modification of a protein after
its translation is known as Post-
Translational Modification.
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Play a crucial role in generating the
heterogeneity in proteins.
Help in utilizing identical proteins for different
cellular functions in different cell types.
Regulation of particular protein sequence
behavior in most of the eukaryotic
organisms.
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Play an important part in modifying the end
product of expression.
Contribute towards biological processes
and diseased conditions.
Translocation of proteins across biological
membranes.
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Trimming
Covalent Modification
Ubiquitination
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Removal of a part of the translated
sequence.
Proteases Protein activation.
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Phosphorylation
Glycosylation
Hydroxylation
Carboxylation
Biotinylation
Acetylation
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Methylation
Alkylation
Glutamylation
Lipoylation
Sulfation
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Phosphorylation
The addition of a phosphate (PO4)
group to a protein or a small molecule.
Can occur on Serine, Threonine,
Tyrosine.
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Glycosylation
The addition of saccharide to a protein
or a lipid molecule.
N-Linked Glycosylation
• Amide nitrogen of Asparagine
O-Linked Glycosylation
• Hydroxyl oxygen of Serine and Therionine.
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Hydroxylation
The addition of hydroxyl group to
proline of protein.
Carboxylation
The addition of carboxyl group to
glutamate.
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Biotinylation
The addition of biotin to protein or
nucleic acid.
Acetylation
The addition of an acetyl group, usually
at the N-terminus of the protein.
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Methylation
The addition of a methyl group, usually
at lysine or arginine residues.
Alkylation
The addition of an alkyl group (e.g.
methyl, ethyl).
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Glutamylation
Covalent linkage of glutamic acid residues
to tubulin and some other
Lipoylation
The attachment of a lipoate functionality
Sulfation
The addition of a sulfate group to a
tyrosine.
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Addition of phosphate group to a protein.
Principally on serine, threonine or tyrosine
residues.
Also known as Phospho regulation.
Critical role in cell cycle, growth, apoptosis
and signal transduction pathways.
Protein kinases
ATP + protein ———————> phosphoprotein + ADP
Phosphorylation
The covalent attachment of
oligosaccharides
Addition of glycosyl group or carbohydrate
group to a protein.
Principally on Asparagine, hydroxylysine,
serine or threonine.
Significant effect on protein folding,
conformation, distribution, stability and
activity.
N-Linked glycans
attached to nitrogen of Asparagine or arginine
side chains.
O-Linked glycans
attached to hydroxy oxygen of serine,threonine
Phospho glycans
linked through the phosphate of serine.
C-Linked glycans
Rare form, Sugar is added to a carbon on
tryptophan side chain.
Nitrosyl (NO) group is added to the
protein.
NO a chemical messenger that reacts with
free cysteine residues to form S-
nitrothiols.
Used by cells to stabilize proteins, regulate
gene expression.
Addition of methyl group to a protein.
Usually at lysine or arginine residues.
Binds on nitrogen and oxygen of proteins
Methyl donor is S-adenosylmethionine
(SAM)
Enzyme for this is methyltransferase
Methylation of lysine residues in histones in
DNA is important regulator of chromatin
structure
Where SAM (S-adenosyl methionine) is converted into SAH(S-adenosyl
homocysteine)
Addition of acetyl group to the nitrogen.
Histones are acetylated on lysine residues in
the N-terminal tail as a part of gene regulation.
Involved in regulation of transcription factors,
effector proteins, molecular chaperons and
cytoskeletal proteins.
Methionine aminopeptidase (MAP) is an
enzyme responsible for N-terminal acetylation
Where,
HDACs = Histone deactyllase ,
KATs = N-acetyltransferase.
Lipidation attachment of a lipid group,
such as a fatty acid, covalently to a protein.
In general, lipidation helps in cellular
localization and targeting signals,
membrane tethering and as mediator of
protein-protein interactions.
C-terminal glycosyl
phosphatidylinositol (GPI) anchor
N-terminal myristoylation
S-palmitoylation
S-prenylation
GPI anchors tether cell surface proteins to
the plasma membrane
GPI-anchored proteins are often localized to
cholesterol- and sphingolipid-rich lipids,
which act as signaling platforms on the
plasma membrane.
It is the attachment of myristoyl group a
14-carbon saturated fatty acid (C14) to a
protein.
It is facilitated by N-myristoyltransferase
(NMT) and uses myristoyl-CoA as the
substrate.
It is addition of C16 palmitoyl group
from palmitoyl-CoA
Palmitoyl acyl transferases (PATs)
enzyme favors this step.
Reversed by thioesterases
Addition of a farnesyl (C15) or
geranylgeranyl (C20) group to proteins.
Enzyme involved in this reaction is
farnesyl transferase (FT) or
geranylgeranyl transferases (GGT I and
II).
Disulfide bonds are covalent bonds formed
between two cysteine residues (R-S-S-R).
These bonds contribute to the correct
folding of proteins as other elements of
secondary structure
Cleavage of peptide bonds by proteases.
Examples of Proteases- Serine Proteases,
Cysteine Proteases, Aspartic acid Proteases.
Involved in Antigen processing, Apoptosis,
Cell signalling
Ubiquitin is a small regulatory protein that
can be attached to the proteins and label
them for destruction.
Effects in cell cycle regulation, control of
proliferation and differentiation,
programmed cell death (apoptosis), DNA
repair, immune and inflammatory processes
and organelle biogenesis.
Highly specific degradation of protein can be
achieved through the addition of one to
several ubiquitin molecules to a target
protein. The process is called Ubiquitination.
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These are particularly important for the study of
heart disease, cancer, neurodegenerative diseases
and diabetes.
These are key mechanisms to increase proteomic
diversity.
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