Bacillus subtilis DEAD Protein YdbR Possesses ATPase, RNA Binding, and RNA Unwinding Activities
The product of an open reading frame (ORF) (called YdbR) identified while analyzing the <I>Bacillus subtilis</I> 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-His<SUB>6</SUB> purified from <I>Escherichia coli</I> is an ATP-independent RNA binding protein. It also possesses RNA-dependent ATPase activity stimulated not only by total RNA from <I>B. subtilis</I> but also by an RNA that is irrelevant to that of <I>B. subtilis</I>. Functional analysis indicated that the growth rate of a Δ<I>ydbR</I> mutant strain of <I>B. subtilis</I> was reduced as compared with that of the wild type not only at 37 °C, but more severely at 22 °C.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(7), 1606-1615, 2006-07-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry