Human RNA helicase A is homologous to the maleless protein of Drosophila Journal Article

Authors: Lee, C. G.; Hurwitz, J.
Article Title: Human RNA helicase A is homologous to the maleless protein of Drosophila
Abstract: 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.
Keywords: nonhuman; animal; gene expression; cell line; drosophila; hela cell; hela cells; transcription factors; nuclear proteins; dna; amino acid sequence; molecular sequence data; sequence homology, amino acid; enzyme analysis; nucleotide sequence; immunoblotting; base sequence; dna sequence; helicase; sequence homology; blotting, northern; rna helicases; insect; baculovirus; moths; rna nucleotidyltransferases; unidentified baculovirus; insecta; human; priority journal; article; support, u.s. gov't, non-p.h.s.
Journal Title: Journal of Biological Chemistry
Volume: 268
Issue: 22
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1993-08-05
Start Page: 16822
End Page: 16830
Language: English
PUBMED: 8344961
PROVIDER: scopus
Notes: Article -- Export Date: 1 March 2019 -- Source: Scopus
Citation Impact
MSK Authors
  1. Jerard Hurwitz
    191 Hurwitz
  2. Chee-Gun   Lee
    11 Lee