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Regulation of Translation
The dephosphorylated eIF: Active form
Heme prevents eIF phosphorylation Heme stimulates translation
Proteins/mRNA interactions:
e.g., Ferritin and transferrin receptor synthesis
Posttranslational Modifications
Trimming
Covalent modifications:Phosphorylation Biotinylation
Glycosylation Farnesylation
Hydroxylation AcetylationCarboxylation
Ubiquitination
Posttranslational Modifications:
Trimming Removal of a part of the translated sequence Proteases protein activation Cellular site of cleavage:
ER and Golgi apparatus
Secretory vesicles: e.g., insulin
After secretion: e.g., collagen
At sites of action: zymogen e.g., trypsinogen
Posttranslational Modifications:
PhosphorylationAddition of phosphate to hydroxyl group of
Serine and threonineTyrosine
Reversible: Addition by kinasesRemoval by phosphatases
Increase or decrease the activity of a specific protein
e.g., Glycogen synthase and glycogen phosphorylase
Posttranslational Modifications:Glycosylation
Modifications of :proteins of plasma membraneproteins of lysosomesecretory proteins
Addition of carbohydrate chains to:Hydroxyl group of serine or threonine (O-linked)Amide group of asparagine (N-linked)
Site: Golgi apparatus and ER
Protein targeting: e.g., mannose-6-phosphate to lysosomal enzymes
Posttranslational Modifications:Hydroxylation
Proline and lysine
Endoplasmic reticulum
Prolyl or lysyl hydroxylases
e.g., Collagen
Posttranslational Modifications:Other Covalent Alterations - 1
Carboxylation:
γ-carboxylation of glutamic acid residue for maturation of vitamin K-dependent clotting factors
II, VII, IX and X
Posttranslational Modifications:Other Covalent Alterations - 2
Biotinylation
Farnesylation
e.g., Acetyl Co-A Carboxylase
e.g., Protein anchoring to membranes