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著作: [矢野 仁康]/S. Mori/[木戸 博]/Intrinsic Nucleoside Diphosphate Kinase-like Activity is a Novel Function of the 20S Proteasome/[The Journal of Biological Chemistry]

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EID
154876
EOID
823867
Map
0
LastModified
2016年7月5日(火) 20:47:31
Operator
大家 隆弘
Avail
TRUE
Censor
0
Owner
木戸 博
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種別 必須 学術論文(審査論文)
言語 必須 英語
招待 推奨
審査 推奨
カテゴリ 推奨
共著種別 推奨
学究種別 推奨
組織 推奨
  1. 徳島大学.分子酵素学研究センター(〜2007年3月31日/->組織[徳島大学.疾患酵素学研究センター])
著者 必須
  1. 矢野 仁康
    役割 任意
    貢献度 任意
    学籍番号 推奨
  2. (英) S. Mori
    役割 任意
    貢献度 任意
    学籍番号 推奨
  3. 木戸 博([徳島大学.先端酵素学研究所.重点研究部門])
    役割 任意
    貢献度 任意
    学籍番号 推奨
題名 必須

(英) Intrinsic Nucleoside Diphosphate Kinase-like Activity is a Novel Function of the 20S Proteasome

副題 任意
要約 任意

(英) 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.

キーワード 推奨
  1. (英) Adenosine Diphosphate
  2. (英) Adenosine Triphosphate
  3. (英) Amino Acid Sequence
  4. (英) Cysteine Endopeptidases
  5. (英) Cytidine Diphosphate
  6. (英) Humans
  7. (英) Kinetics
  8. (英) Molecular Sequence Data
  9. (英) Multienzyme Complexes
  10. (英) Nucleoside-Diphosphate Kinase
  11. (英) Peptide Fragments
  12. (英) Phosphorylation
  13. (英) Proteasome Endopeptidase Complex
  14. (英) Sequence Analysis, Protein
  15. (英) Substrate Specificity
  16. (英) Tumor Cells, Cultured
発行所 推奨
誌名 必須 The Journal of Biological Chemistry([The American Society for Biochemistry and Molecular Biology])
(pISSN: 0021-9258, eISSN: 1083-351X)
ISSN 任意 0021-9258
ISSN: 0021-9258 (pISSN: 0021-9258, eISSN: 1083-351X)
Title: The Journal of biological chemistry
Title(ISO): J Biol Chem
Publisher: American Society for Biochemistry and Molecular Biology
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
必須 274
必須 48
必須 34375 34382
都市 任意
年月日 必須 1999年 4月 12日
URL 任意
DOI 任意 10.1074/jbc.274.48.34375    (→Scopusで検索)
PMID 任意 10567415    (→Scopusで検索)
NAID 任意
WOS 任意
Scopus 任意
評価値 任意
被引用数 任意
指導教員 推奨
備考 任意
  1. (英) Article.PublicationTypeList.PublicationType: Journal Article

  2. (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't