論文

査読有り
2004年5月

Dbp9p, a member of the DEAD box protein family, exhibits DNA helicase activity

JOURNAL OF BIOLOGICAL CHEMISTRY
  • T Kikuma
  • ,
  • M Ohtsu
  • ,
  • T Utsugi
  • ,
  • S Koga
  • ,
  • K Okuhara
  • ,
  • T Eki
  • ,
  • F Fujimori
  • ,
  • Y Murakami

279
20
開始ページ
20692
終了ページ
20698
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M400231200
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

The yeast Dbp9p is a member of the DEAD box family of RNA helicases, which are thought to be involved in RNA metabolism. Dbp9p seems to function in ribosomal RNA biogenesis, but it has not been biochemically characterized. To analyze the enzymatic characteristics of the protein, we expressed a recombinant Dbp9p in Escherichia coli and purified it to homogeneity. The purified protein exhibited RNA unwinding and binding activity in the absence of NTP, and this activity was abolished by a mutation in the RNA-binding domain. We then characterized the ATPase activity of Dbp9p with respect to cofactor specificity; the activity was found to be severely inhibited by yeast total RNA and moderately inhibited by poly(U), poly(A), and poly(C) but to be stimulated by yeast genomic DNA and salmon sperm DNA. In addition, Dbp9p exhibited DNA-DNA and DNA-RNA helicase activity in the presence of ATP. These results indicate that Dbp9p has biochemical characteristics unique among DEAD box proteins.

リンク情報
DOI
https://doi.org/10.1074/jbc.M400231200
CiNii Articles
http://ci.nii.ac.jp/naid/80016695083
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/15028736
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000221273800020&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M400231200
  • ISSN : 0021-9258
  • CiNii Articles ID : 80016695083
  • PubMed ID : 15028736
  • Web of Science ID : WOS:000221273800020

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