Nucleic Acids Research, Vol 26, Issue 11 2638-2643, Copyright © 1998 by Oxford University Press
M Okanami, T Meshi and M Iwabuchi
We have isolated cDNAs encoding a novel member of the DEAD box RNA helicase
family from Arabidopsis. The protein, named AtDRH1, is composed of 619
amino acids and the central portion has high similarity with the helicase
core region of a prototypic RNA helicase, the human nuclear protein p68.
The N- and C-terminal regions are considerably diverged from the animal and
yeast p68 homologs at the amino acid sequence level, but like the p68
subfamily members, an RGG box-like domain is present near the C-terminus.
RNA blot analysis showed that the AtDRH1 transcript accumulates at a high
level and almost equally in every part of the Arabidopsis plant. The
purified, recombinant AtDRH1 was capable of unwinding double-stranded RNA
in the presence of ATP or dATP and of hydrolyzing ATP. The ATPase activity
was stimulated by some single-stranded RNAs and DNAs, including poly(A) and
poly(dT), but not by poly(dA). The ability of the polynucleotides to
stimulate the ATPase activity was largely consistent with their affinity
for AtDRH1. These results show that AtDRH1 is a novel type of
ATP/dATP-dependent RNA helicase and polynucleotide-dependent ATPase.
ARTICLES
Characterization of a DEAD box ATPase/RNA helicase protein of Arabidopsis thaliana
Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
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