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Prokaryotic ubiquitin-like protein : ウィキペディア英語版 | Prokaryotic ubiquitin-like protein Prokaryotic ubiquitin-like protein (Pup) - functional analog of ubiquitin found in Prokaryote (Mycobacterium tuberculosis). Serves the same function, although the enzymology of ubiquitylation and pupylation is different. In contrast to the three-step reaction of ubiquitylation, pupylation requires two steps, therefore only two enzymes are involved in pupylation. Similar to ubiquitin, Pup attaches to specific lysine residues of substrate proteins by forming isopeptide bonds, then recognized by Mycobacterium proteasomal ATPase(Mpa) by binding-induced folding mechanism〔Wang T, Darwin KH, Li H. Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation.''Nat Struct Mol Biol''. 2010 Nov;17(11):1352-7. (doi: 10.1038/nsmb.1918 ).〕 to form the unique alpha-helix, then Mpa deliver the Pup-substrate to 20S proteasome by coupling of ATP hydrolysis for proteasomal degradation. Therefore, like eukaryotes, bacteria may use a small-protein modifier to control protein stability. The X-ray crystal structure of Pup/Mpa complex (PDB:(3M9D ))was firstly determined by scientists Tao Wang and Huilin Li in (Brookhaven National Laboratory, USA ). Pup gene encode a 64–amino acid protein with a molecular size of 6.944-kDa: ==Database== PupDB is a database of pupylated proteins and pupylation sites
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