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PTMs
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Table Contents
 Definition
 Introduction
 Components of PTMs
 Conclusion
2
Definition
Protein post-translational modifications (PTMs)
increase the functional diversity of the proteome
by the covalent addition of functional groups or
proteins, proteolytic cleavage of regulatory
subunits, or degradation of entire proteins.
3
Introduction
• These modifications include phosphorylation,

glycosylation, ubiquitination, nitrosylation,
methylation, acetylation, lipidation and
proteolysis and influence almost all aspects of
normal cell biology and pathogenesis.
• Therefore, identifying and understanding
PTMs is critical in the study of cell biology and
disease treatment and prevention.
4
5
Components of PTMs
Phosphorylation
• Reversible protein phosphorylation, principally
on serine, threonine or tyrosine residues, is one
of the most important and well-studied post-
translational modifications.
• Phosphorylation plays critical roles in the
regulation of many cellular processes, including
cell cycle, growth, apoptosis and signal
transduction pathways.
●●●
6
Components of PTMs
Glycosylation
• Protein glycosylation is acknowledged as one of
the major post-translational modifications, with
significant effects on protein folding,
conformation, distribution, stability and activity.
• Glycosylation encompasses a diverse selection of
sugar-moiety additions to proteins that ranges
from simple monosaccharide modifications of
nuclear transcription factors to highly complex
branched polysaccharide changes of cell surface
receptors. ●●●
7
Components of PTMs
Ubiquitination
• Ubiquitin is an 8-kDa polypeptide consisting of 76
amino acids that is appended to the Îµ-NH2 of lysine
in target proteins via the C-terminal glycine of
ubiquitin.
• Following an initial monoubiquitination event, the
formation of a ubiquitin polymer may occur, and
polyubiquitinated proteins are then recognized by
the 26S proteasome that catalyzes the degradation
of the ubiquitinated protein and the recycling of
ubiquitin.
●●●
8
Components of PTMs
S-nitrosylation
• Nitric oxide (NO) is produced by three
isoforms of nitric oxide synthase (NOS),
and it is a chemical messenger that reacts
with free cysteine residues to form S-
nitrothiols (SNOs).
●●●
9
Components of PTMs
Methylation
• The transfer of one-carbon methyl groups to
nitrogen or oxygen (N- and O-methylation,
respectively) to amino acid side chains
increases the hydrophobicity of the protein
and can neutralize a negative amino acid
charge when bound to carboxylic acids.
●●●
10
Components of PTMs
N-acetylation
• N-acetylation, or the transfer of an acetyl group
to nitrogen, occurs in almost all eukaryotic
proteins through both irreversible and reversible
mechanisms.
• N-terminal acetylation requires the cleavage of
the N-terminal methionine by methionine
aminopeptidase (MAP) before replacing the
amino acid with an acetyl group from acetyl-CoA
by N-acetyltransferase (NAT) enzymes.
●●●
11
Components of PTMs
Lipidation
• Lipidation is a method to target proteins
to membranes in organelles (endoplasmic
reticulum [ER], Golgi apparatus,
mitochondria), vesicles (endosomes,
lysosomes) and the plasma membrane.
●●●
12
Components of PTMs
Proteolysis
• Peptide bonds are indefinitely stable under
physiological conditions, and therefore cells
require some mechanism to break these
bonds.
• Proteases comprise a family of enzymes that
cleave the peptide bonds of proteins and are
critical in antigen processing, apoptosis,
surface protein shedding and cell signaling.
13
14
Conclusion
 Posttranslational modifications (PTMs) are

covalent processing events that change the
properties of a protein by proteolytic cleavage
and adding a modifying group, such as acetyl,
phosphoryl, glycosyl and methyl, to one or more
amino acids.
15
References
• Google.com
• Wikipedia.org
• Studymafia.org
• Slidespanda.com
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• These modifications include phosphorylation,

 Posttranslational modifications (PTMs) are

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