Nucleic Acids Research, Vol 27, Issue 19 3811-3820, Copyright © 1999 by Oxford University Press
K Kossen and OC Uhlenbeck
DEAD, DEAH and DExH proteins are involved in almost every facet of RNA
biochemistry. Members of these protein families exhibit an RNA- dependent
ATPase activity and some possess an ATP-dependent RNA helicase activity.
Although genetic studies have identified specific functions for certain
DEx(D)/(H)proteins from which an RNA substrate can be reasonably inferred,
only DbpA from Escherichia coli has been shown to exhibit significant RNA
specificity in vitro. Here we describe the characterization of YxiN from
Bacillus subtilis, the second DEx(D)/(H)protein to show significant RNA
specificity as an isolated, homogenous protein. The ATPase activity of
YxiN, like that of DbpA, is stimulated by a 154 nt fragment of 23S rRNA.
YxiN has a 2 nM apparent binding constant for this fragment, yet its ATPase
activity shows 1800- fold RNA specificity. Along with the conserved motifs
shared among all DEAD proteins, YxiN and DbpA have a conserved C-terminal
extension. This extension is highly conserved in several additional DEAD
proteins. We propose that the C-terminus identifies a protein sub-family
whose members bind 23S rRNA and that proteins of this family are likely to
function in rRNA maturation/ribosome biogenesis or an unappreciated aspect
of translation.
ARTICLES
Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: delineation of a novel sub-family of bacterial DEAD proteins
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA.
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