Protein Modification Flashcards
N-Acetylation
from acetyl coA, in histones, relax association w DNA making available for transcription. Uses MAP to cut N off, NAT gives acetyl to lysine. MAP-NAT
Acylation
attachment of FA, in small g-proteins w palmitic acid or myristic acid affects attachment to subcellular membrane
ADP Ribosylation
Bacterial toxins (cholera, diphtheria, salmonella) ADP ribosylate target proteins such as G proteins
Carboxylation
Attachment of carboxyl (COOH), Vit K dependent clotting factors are activated via carboxylation
Disulfide bonds
Ox of sulfhydryl (SH) to disulfide (S-S) for stabilization of protein structure
Glycation and glycosylation
Non enzymatic attachment of glucose, such as high levels of glycosylated by glycosyltransferases hemoglobin in poorly treated diabetics, glycosylation of bilirubin to make more water soluble for elimination. or glycosylation of erythrocyte membrane defines blood type.
Happens in ER and Golgi. Needs UDP sugar
GPI (glycosylphosphatidylinositol)
GPI-linked proteins are attached to plasma membrane outer surface
Hydroxylation
Vit C dependent hydroxylation of proline and lysine are essential for stable collagen
Methylation
Methylation of histones tightens w DNA more, inhibiting DNA transcription
Phosphorylation
By kinase or phosphatase is used to activate or inhibit function, often in cell signaling cascade
Lipidation (Prenylation)
Lipidation of protein anchors them to inner plasma membrane
Sulfation
attachment of sulfate group on fibrinogen (protein involved in coagulation) and gastrin (gastric acid secretion)
Ubiquitination
Adding ubiquiting tags a protein for degradation by protease
Hydrophilic PTMs
Hydroxylation, Phosphorylation, Glycosylation
Hydrophobic PTMs
Methylation and Lipidation