Bacillus subtilis DEAD Protein YdbR Possesses ATPase, RNA Binding, and RNA Unwinding Activities

• ANDO Yoshinari

  Graduate School of Life and Environmental Sciences, University of Tsukuba

• NAKAMURA Kouji

  Graduate School of Life and Environmental Sciences, University of Tsukuba

Bibliographic Information

Other Title

• <i>Bacillus subtilis</i>DEAD Protein YdbR Possesses ATPase, RNA Binding, and RNA Unwinding Activities

Abstract

The product of an open reading frame (ORF) (called YdbR) identified while analyzing the Bacillus subtilis genome has been classified as an Asp-Glu-Ala-Asp (DEAD) protein, but the biological function and enzymology of YdbR have not been characterized in detail. Here we show that recombinant YdbR-His₆ purified from Escherichia coli is an ATP-independent RNA binding protein. It also possesses RNA-dependent ATPase activity stimulated not only by total RNA from B. subtilis but also by an RNA that is irrelevant to that of B. subtilis. Functional analysis indicated that the growth rate of a ΔydbR mutant strain of B. subtilis was reduced as compared with that of the wild type not only at 37 °C, but more severely at 22 °C.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 70 (7), 1606-1615, 2006

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• RNA helicase
• Asp-Glu-Ala-Asp (DEAD) protein
• <I>Bacillus subtilis</I>
• cold shock

Details

• CRID: 1390282681456563456
• NII Article ID: 10018528883
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.50678
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 7997781
• Web Site: http://id.ndl.go.jp/bib/7997781
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I7997781
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.50678
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed