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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1993-9-7
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pubmed:databankReference |
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pubmed:abstractText |
RNA helicase A is an abundant nuclear enzyme of HeLa cells that unwinds double-stranded RNA in a 3' to 5'direction (Lee, C. G., and Hurwitz, J. (1992) J. Biol. Chem. 267, 4398-4407). A complementary DNA (cDNA) clone expressing RNA helicase A was isolated by screening a human cDNA library with polyclonal antibodies produced against the purified protein. The deduced amino acid sequence from this clone showed that RNA helicase A is a member of the DEAH family of proteins thought to be helicases. Sequence comparison among all known proteins of the DEAH family revealed that the highest homology was between RNA helicase A and the maleless protein (MLE) of Drosophila. There was 49% identity and 85% similarity throughout the overall primary sequences of both proteins, suggesting that RNA helicase A is the human counterpart of Drosophila MLE. Polyclonal antibodies against Drosophila MLE recognized RNA helicase A in crude nuclear extracts of HeLa cells as well as the purified protein. A recombinant RNA helicase A containing 6 histidine residues at the NH2 terminus was expressed in Sf9 cells using a baculovirus vector. The protein isolated from insect cells and the enzyme purified from HeLa cells exhibited identical RNA helicase and RNA-dependent ATPase activities.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/mle protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:geneSymbol |
mle
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16822-30
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pubmed:dateRevised |
2008-10-15
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pubmed:meshHeading |
pubmed-meshheading:8344961-Amino Acid Sequence,
pubmed-meshheading:8344961-Animals,
pubmed-meshheading:8344961-Base Sequence,
pubmed-meshheading:8344961-Blotting, Northern,
pubmed-meshheading:8344961-Cell Line,
pubmed-meshheading:8344961-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:8344961-DNA,
pubmed-meshheading:8344961-DNA Helicases,
pubmed-meshheading:8344961-DNA-Binding Proteins,
pubmed-meshheading:8344961-Drosophila,
pubmed-meshheading:8344961-Drosophila Proteins,
pubmed-meshheading:8344961-HeLa Cells,
pubmed-meshheading:8344961-Humans,
pubmed-meshheading:8344961-Immunoblotting,
pubmed-meshheading:8344961-Molecular Sequence Data,
pubmed-meshheading:8344961-Moths,
pubmed-meshheading:8344961-Nuclear Proteins,
pubmed-meshheading:8344961-RNA Helicases,
pubmed-meshheading:8344961-RNA Nucleotidyltransferases,
pubmed-meshheading:8344961-Sequence Homology, Amino Acid,
pubmed-meshheading:8344961-Transcription Factors
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pubmed:year |
1993
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pubmed:articleTitle |
Human RNA helicase A is homologous to the maleless protein of Drosophila.
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pubmed:affiliation |
Graduate Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, New York, New York 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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