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    Post-Translational Modification: Myristoylation Palmitoylation

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    AlanCheval
    Post-translational modification (PTM) refers to the processes that proteins undergo after they are translated from mRNA to polypeptide chains. These modifications include folding, cutting, and the addition of other biochemical groups. PTMs help proteins mature and determine their final structure and function. They allow proteins to take on new activities like enzymatic activation or targeting to specific cellular locations. Common PTMs include phosphorylation, acetylation, glycosylation, and the formation of disulfide bridges. A variety of techniques can detect PTMs, such as mass spectrometry.

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    Post-Translational Modification: Myristoylation Palmitoylation

    Uploaded by

    AlanCheval
    113 views2 pages
    Post-translational modification (PTM) refers to the processes that proteins undergo after they are translated from mRNA to polypeptide chains. These modifications include folding, cutting, and the addition of other biochemical groups. PTMs help proteins mature and determine their final structure and function. They allow proteins to take on new activities like enzymatic activation or targeting to specific cellular locations. Common PTMs include phosphorylation, acetylation, glycosylation, and the formation of disulfide bridges. A variety of techniques can detect PTMs, such as mass spectrometry.

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    Posttranslational Modification

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    Posttranslational Modification

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    Post-translational modification (PTM) refers to the processes that proteins undergo after they are translated from mRNA to polypeptide chains. These modifications include folding, cutting, and the addition of other biochemical groups. PTMs help proteins mature and determine their final structure and function. They allow proteins to take on new activities like enzymatic activation or targeting to specific cellular locations. Common PTMs include phosphorylation, acetylation, glycosylation, and the formation of disulfide bridges. A variety of techniques can detect PTMs, such as mass spectrometry.

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    113 views2 pages

    Post-Translational Modification: Myristoylation Palmitoylation

    Uploaded by

    AlanCheval
    Post-translational modification (PTM) refers to the processes that proteins undergo after they are translated from mRNA to polypeptide chains. These modifications include folding, cutting, and the addition of other biochemical groups. PTMs help proteins mature and determine their final structure and function. They allow proteins to take on new activities like enzymatic activation or targeting to specific cellular locations. Common PTMs include phosphorylation, acetylation, glycosylation, and the formation of disulfide bridges. A variety of techniques can detect PTMs, such as mass spectrometry.

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    Post-translational Modification

    Posttranslational modification (PTM) is a step in protein biosynthesis. Proteins


    are created by ribosomes translating mRNA into polypeptide chains. These
    polypeptide chains undergo PTM (such as folding, cutting and other processes)
    before becoming the mature protein product.
    After translation, the posttranslational modification of amino acids extends the
    range of functions of the protein by attaching it to other biochemical functional
    groups (such as acetate, phosphate, various lipids and carbohydrates), changing
    the chemical nature of an amino acid (e.g. citrullination), or making structural
    changes (e.g. formation of disulfide bridges).
    Also, enzymes may remove amino acids from the amino end of the protein, or cut
    the peptide chain in the middle. For instance, the peptide hormone insulin is cut
    twice after disulfide bonds are formed, and a propeptide is removed from the
    middle of the chain; the resulting protein consists of two polypeptide chains
    connected by disulfide bonds.
    Other modifications, like phosphorylation, are part of common mechanisms for
    controlling the behavior of a protein, for instance activating or inactivating an
    enzyme.
    Also, most nascent polypeptides start with the amino acid methionine because
    the "start" n mRNA also codes for this amino acid. This amino acid is usually
    removed during post-translational modification.
    Post-translational modification of proteins can be detected by a variety of
    techniques, including mass spectrometry, Eastern blotting, and Western
    blotting.
    # PTMs involving addition of hydrophobic groups:
    To target proteins to membranes in organelles (endoplasmic reticulum,
    Golgi apparatus, mitochondria), vesicles (endosomes, lysosomes) and the
    plasma membrane.
    Myristoylation, attachment of myristate, a C14 saturated acid.
    Palmitoylation, attachment of palmitate, a C16 saturated acid.
    # PTMs involving addition of cofactors:
    To enhance enzymatic activity.
    Lipoylation, attachment of a lipoate (C8) functional group.

    Covalent attachment of flavin moiety (FMN or FAD).

    # PTMs involving unique modifications of translation factors:


    Diphthamide formation (on a histidine found in eEF2).
    Ethanolamine phosphoglycerol attachment (on glutamte found in eEF1).
    # PTMs involving addition of smaller chemical groups:
    Acetylation, the addition of an acetyl group.
    Glycosylation, the addition of a glycosyl group.
    Methylation, the addition of a methyl group.
    Phosphorylation, the addition of a phosphate group.
    # PTMs involving non-enzymatic additions:
    Glycation, the addition of a sugar molecule (impairs functioning of
    protein).
    Biotinylation, the addition of a biotin molecule (doesnt impair functioning
    of protein).
    # PTMs involving addition of other proteins or peptides:
    Ubiquitination, the covalent linkage to the protein ubiquitin.
    ISGylation, the covalent linkage to the ISG15 protein (InterferonStimulated Gene 15).
    # PTMs involving change in the chemical nature of amino acids:
    Citrullination, the conversion of arginine to citrulline.
    Carbamylation, the conversion of lysine to homocitrulline.
    # PTMs involving structural changes:
    Disulfide bridges, the covalent linkage of two cysteine amino acids.
    Proteolytic cleavage, cleavage of a protein at a peptide bond.

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