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 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-His(6) 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 DeltaydbR mutant strain of B. subtilis was reduced as compared with that of the wild type not only at 37 degrees C, but more severely at 22 degrees C.
Ando
Yoshinari
Y
Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba-shi, Ibaraki 305-8572, Japan.
Nakamura
Kouji
K
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000254:growth & development / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D016680:Genome, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D020365:RNA Helicases / Q000235:genetics / Q000378:metabolism*; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D012329:RNA, Bacterial; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D020365:RNA Helicases