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PMID: 8041617 Published · ppublish English Journal Article

Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: implications for monomeric RNA helicases.

Nucleic acids research ·Vol. 22 ·No. 13 ·1994-07-11 ·Pages 2552-6

Gibson TJ, Thompson JD

Abstract

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 RNA-binding capacity must be supplied either as domains adjacent to the DEAD/DExH-box or by bound partners as in the eIF-4AB dimer. The presence or absence of extra RNA-binding domains should allow classification of DEAD/DExH proteins as monomeric or multimeric helicases.

MeSH Terms
Amino Acid Sequence Animals Chromosomal Proteins, Non-Histone DNA Helicases DNA-Binding Proteins Databases, Factual Drosophila/enzymology,genetics Drosophila Proteins Humans Male Molecular Sequence Data Nuclear Proteins/metabolism RNA Helicases RNA Nucleotidyltransferases/metabolism RNA, Double-Stranded/metabolism Repetitive Sequences, Nucleic Acid Sequence Homology, Amino Acid Transcription Factors/metabolism
Chemicals
Chromosomal Proteins, Non-Histone DNA-Binding Proteins Drosophila Proteins Nuclear Proteins RNA, Double-Stranded Transcription Factors mle protein, Drosophila RNA Nucleotidyltransferases DNA Helicases RNA Helicases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gibson T J
European Molecular Biology Laboratory, Heidelberg, Germany.
Thompson J D
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/22.13.2552
Published
1994-07-11
Pages
2552-6
Language
English
Region
England
NLM ID
0411011
PMCID
PMC308209
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/22.13.2552 PMC Full Text View journal details
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