生物化学蛋白质部分讲解2.pptx

Protein Ubiquitination and Degradation;Protein Degradation Why are proteins degraded? In order to keep a cell working it needs to remove: incorrectly synthesized proteins (with errors in amino acid sequence) damaged proteins (i.e. oxidative damage) cell-cycle specific proteins other signaling proteins which are no longer necessary Protein degradation could occur in the cytoplasm, nucleus, chloroplast, mitochondria, Vacuole (lysosome) and even in the intracellular space Lysosomes are acidic vesicles that contain about 50 different enzymes involved in degradation: proteases (cathepsins):? cleave peptide bonds phosphatases:? remove covalently bound phosphates nucleases:? cleave DNA/RNA lipases:? cleave lipid molecules carbohydrate-cleaving enzymes:? remove covalently bound sugars from glycoproteins Lysosomes often secrete their contents into the extracellular medium via exocytosis. Lysosomes can also target damaged organelles in a process called autophagy. Sometimes, lysosomes are triggered to rupture inside a cell, resulting in autolysis, also called apoptosis or programmed cell death.;(Buchanan et al. Biochem and Mol Biol of Plants, ASPP);Cysteine proteases (CP) (106 genes in Arabidopsis) Phytocalpain= regulatory role in embryonic pattern formation and SAM formation, cell fate specification in the endosperm and leaf epidermis, and regulation of the balance between cell differentiation and proliferation. Only one gene, striking difference with animals. Papain was the first model cysteine protease. Papain-like enzymes are involved in protein degradation and N-mobilization during seed germination, leaf senescence and cell death events, plant resistance against pathogens and insects. Legumains are the most intensively studied. They are also called asparaginyl-endopeptidases or vacuolar processing enzymes (VPEs) and are involved in the processing of seed storage proteins and have been implicated in storage protein breakdown and tissue senescence. defective kernel 1 in