Nucleic Acids Research, 1994, Vol. 22, No. 13 2552-2556
© 1994
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Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: implications for monomeric RNA helicases
European Molecular Biology Laboratory Postfach 102209, Meyerhofstrasse 1, D69012 Heidelberg, Germany
*To whom correspondence should be addressed
Received March 31, 1994. Revised May 31, 1994. Accepted May 31, 1994.
Searches with dsRNA-binding domain profiles detected two copies of the domain in each of RNA helicase A, Drosophila maleless and C.elegans ORF T20G5_11 (of unknown function). RNA helicase A is unusual in being one of the few characterised DEAD/DExH helicases that are active as monomers. Other monomeric DEAD/DExH RNA helicases (p68, NPH-II) have domains that match another RNA-binding motif, the RGG repeat. The DEAD/DExH domain appears to be insufficient on its own to promote helicase activity and additional RNAbinding capacity must be supplied either as domains adjacent to the DEAD/DExH-box or by bound partners as in the elF-4AB dimer. The presence or absence of extra RNA-binding domains should allow classification of DEAD/DExH proteins as monomeric or multimeric helicases.
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