POST TRANSLATION
MODIFICATION(COVALENT
MODIFICATION)
-GENE EXPRESSION IN EUKARIYOTES
NAME: DHRUVI SUVAGIYA
CLASS:MSC SEM 3
A LITTLE BACKGROUND –
GENE EXPRESSION
IN EUKARYOTES
WHAT IS POST TRANSLATION
MODIFICATION??
• Post-translational modification (PTM) refers to the covalent and
generally enzymatic modification of proteins
• Proteins are synthesized by ribosomes translating mRNA into
polypeptide chains, which may then undergo PTM to form the
mature protein product.
• Post-translational modifications can occur on the amino acid side
chains or at the protein's C- or N- terminal.
• They can extend the 20 standard amino acids by modifying an
existing functional group or introducing a new one such
as phosphate, methane, lipid residues,etc.for regulating the activity
of enzymes and is the most common post-translational.
WHY PTMs ARE NECESSARY??
• 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 behaviour in most of
the eukaryotic organisms.
• Play an important part in modifying the end product of
expression.
• Contribute towards biological processes and diseased
conditions.
• Translation of proteins across biological membranes.
TYPES OF PTMs??
PTMs TYPES
TRIMMING
COVALENT
MODIFICATION
UBIQUITINATION
COVALENT BOND MODIFICATION
• The proteins synthesized in translation are subjected to many
covalent changes.
• By these modifications in the amino acids the proteins may be
converted to active form or inactive form.
• These including,..
phosphorylation,
glcosylation,
methylation,
alkaylation,
lipoylation,
sulfation,
Carboxylation,
acetylation.
Phosphorylation
• Addition of phosphate group to protein.
• Principally on serine, threonine or tyrosine residues.
• Also known as phospho regulation
• Play crucial role in cell growth, cell cycle, apoptosis and
signal transduction.
Glycosylation
• The covalent attachment of oligosaccharides
• Addition of glycol group to protein.
• Principally on aspargine,hydroxylysine,serine or threonine.
• Play role in protein folding, conformation, distribution,
stability and protein activity.
Methylation
• Addition of methyl group to protein
• Usually at lysine or arginine residues,
• Binds on nitrogen and oxygen of proteins
• Play role in histone methylation –important regulator of
chromatin structure.
N-Acylation
• Addition of acetyl group at nitrogen group.
• Histone are acetylated on lysis residues in the n terminal tail as
a part of gene regulation.
• Play role in regulation of transcription factors, effector
proteins, molecular chaperon and cytoskeletoetal proteins.
• Methionine amino peptidase is an enzyme responsible for n
terminal acetylation.
Disulphide bonding
• Covalent bond formed between two cysteine residues(R-S-S-
R)
• These bonds contribute to the correct folding of protein as
other elements of secondary structure.
Lipidation
• Attachment of lipid group (fatty acid)covalently to protein
• Play role in cellular localization, targeting signals, membrane
structure and protein interactions.
DETECTION TECHNIQUE??
• Mass spectrometry
• HPLC analysis
• Incorporation of radioactive group by addition to growing cell
(75se labelling)
• Antibody cross reactivity(ab against phosphotyrosine)
• Gel electrophoresis.
REFFRENCES
• https://en.wikipedia.org/wiki/Post-
translational_modification#:~:text=Post%2Dtranslational%20
modification%20(PTM),of%20proteins%20following%20prot
ein%20biosynthesis.&text=Other%20forms%20of%20post%2
Dtranslational,removing%20the%20initiator%20methionine%
20residue.
• https://www.nature.com/articles/cr2013151
• https://microbenotes.com/post-translational-modification/
Post translation control-regulation_of_gene_expression_in_eukaryotes - copy

Post translation control-regulation_of_gene_expression_in_eukaryotes - copy

  • 1.
    POST TRANSLATION MODIFICATION(COVALENT MODIFICATION) -GENE EXPRESSIONIN EUKARIYOTES NAME: DHRUVI SUVAGIYA CLASS:MSC SEM 3
  • 2.
    A LITTLE BACKGROUND– GENE EXPRESSION IN EUKARYOTES
  • 3.
    WHAT IS POSTTRANSLATION MODIFICATION?? • Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins • Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product. • Post-translational modifications can occur on the amino acid side chains or at the protein's C- or N- terminal. • They can extend the 20 standard amino acids by modifying an existing functional group or introducing a new one such as phosphate, methane, lipid residues,etc.for regulating the activity of enzymes and is the most common post-translational.
  • 4.
    WHY PTMs ARENECESSARY?? • 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 behaviour in most of the eukaryotic organisms. • Play an important part in modifying the end product of expression. • Contribute towards biological processes and diseased conditions. • Translation of proteins across biological membranes.
  • 5.
    TYPES OF PTMs?? PTMsTYPES TRIMMING COVALENT MODIFICATION UBIQUITINATION
  • 6.
    COVALENT BOND MODIFICATION •The proteins synthesized in translation are subjected to many covalent changes. • By these modifications in the amino acids the proteins may be converted to active form or inactive form. • These including,.. phosphorylation, glcosylation, methylation, alkaylation, lipoylation, sulfation, Carboxylation, acetylation.
  • 8.
    Phosphorylation • Addition ofphosphate group to protein. • Principally on serine, threonine or tyrosine residues. • Also known as phospho regulation • Play crucial role in cell growth, cell cycle, apoptosis and signal transduction.
  • 9.
    Glycosylation • The covalentattachment of oligosaccharides • Addition of glycol group to protein. • Principally on aspargine,hydroxylysine,serine or threonine. • Play role in protein folding, conformation, distribution, stability and protein activity.
  • 10.
    Methylation • Addition ofmethyl group to protein • Usually at lysine or arginine residues, • Binds on nitrogen and oxygen of proteins • Play role in histone methylation –important regulator of chromatin structure.
  • 11.
    N-Acylation • Addition ofacetyl group at nitrogen group. • Histone are acetylated on lysis residues in the n terminal tail as a part of gene regulation. • Play role in regulation of transcription factors, effector proteins, molecular chaperon and cytoskeletoetal proteins. • Methionine amino peptidase is an enzyme responsible for n terminal acetylation.
  • 12.
    Disulphide bonding • Covalentbond formed between two cysteine residues(R-S-S- R) • These bonds contribute to the correct folding of protein as other elements of secondary structure.
  • 13.
    Lipidation • Attachment oflipid group (fatty acid)covalently to protein • Play role in cellular localization, targeting signals, membrane structure and protein interactions.
  • 14.
    DETECTION TECHNIQUE?? • Massspectrometry • HPLC analysis • Incorporation of radioactive group by addition to growing cell (75se labelling) • Antibody cross reactivity(ab against phosphotyrosine) • Gel electrophoresis.
  • 15.