| Intrinsic nucleoside diphosphate kinase-like activity is a novel function of the 20 S proteasome. | |
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MedLine Citation:
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PMID: 10567415 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The eukaryotic 20 S proteasome is the prototype of a new family of the N-terminal nucleophil hydrolases and is composed of numerous low molecular mass subunits arranged in a stack of four rings, each containing seven different alpha- or beta-subunits. Among the beta-type subunits in the yeast proteasome, three proteolytically active ones were identified, although the functions of the other beta- and alpha-type subunits remain to be clarified. We report here that the purified 20 S proteasome exhibits intrinsic nucleoside diphosphate (NDP) kinase-like activity. The proteasome exhibited a preference for ATP and dATP as phosphate donors, and a broad specificity for NDPs, other than GDP, as phosphate acceptors, unlike conventional NDP kinase, which catalyzes the transfer of gamma-phosphate between NDPs and nucleoside triphosphates. During the transfer of gamma-phosphate, the proteasome formed acid-labile phosphohistidine as autophosphorylated intermediates, and NDP-dependent dephosphorylation of the latter then occurred. These enzymatic properties are similar to those of the molecular chaperone, Hsp70, which also exhibits intrinsic NDP kinase-like activity, instead of ATPase activity. C5 among the beta-type subunits and C8 among the alpha-type subunits were autophosphorylated during the gamma-phosphate transfer reaction and were photoaffinity labeled with 8-azido-[alpha-(32)P]ATP, suggesting that the C5 and C8 subunits of the proteasome are responsible for the NDP kinase-like activity. |
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Authors:
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M Yano; S Mori; H Kido |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 274 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1999 Nov |
Date Detail:
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Created Date: 1999-12-29 Completed Date: 1999-12-29 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 34375-82 Citation Subset: IM |
Affiliation:
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Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Diphosphate
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metabolism Adenosine Triphosphate / metabolism Amino Acid Sequence Cysteine Endopeptidases / metabolism* Cytidine Diphosphate / physiology Humans Kinetics Molecular Sequence Data Multienzyme Complexes / metabolism* Nucleoside-Diphosphate Kinase / chemistry, metabolism* Peptide Fragments / chemistry, metabolism Phosphorylation Proteasome Endopeptidase Complex Sequence Analysis, Protein Substrate Specificity Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Multienzyme Complexes; 0/Peptide Fragments; 56-65-5/Adenosine Triphosphate; 58-64-0/Adenosine Diphosphate; 63-38-7/Cytidine Diphosphate; EC 2.7.4.6/Nucleoside-Diphosphate Kinase; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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