A putative mammalian RNA helicase with an arginine-serine-rich domain colocalizes with a splicing factor

J Biol Chem. 1995 Jun 30;270(26):15702-6. doi: 10.1074/jbc.270.26.15702.

Abstract

We have cloned a rat cDNA whose deduced primary structure yields a protein of 117.4 kDa. Because this protein contains RNA helicase consensus motifs, among them a "DEAD" box, we have termed it HEL117 (for helicase of 117.4 kDa). Besides the helicase consensus motifs, HEL117 contains an arginine-serine (RS)-rich domain, which occurs in some proteins involved in RNA splicing. Moreover, the COOH-terminal region of 78 residues of HEL117 is 38.5% identical and 59% similar to the COOH-terminal region of a yeast PRP5 protein that is involved in RNA splicing. Rabbit antibodies generated against a synthetic peptide of HEL117 identified a single polypeptide not only in rat cells but also in cells of other mammals as well as chicken. The antibodies revealed a finely punctate and speckled intranuclear staining in immunofluorescence microscopy. A monoclonal antibody against a human splicing factor containing an RS domain (SC35) showed, in double immunofluorescence microscopy, largely overlapping staining consistent with HEL117 being involved in RNA splicing.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine
  • Base Sequence
  • DNA, Complementary / isolation & purification
  • Humans
  • Molecular Sequence Data
  • RNA Helicases
  • RNA Nucleotidyltransferases / chemistry*
  • RNA Nucleotidyltransferases / genetics
  • RNA Nucleotidyltransferases / immunology
  • RNA Splicing*
  • Rats
  • Serine

Substances

  • DNA, Complementary
  • Serine
  • Arginine
  • RNA Nucleotidyltransferases
  • RNA Helicases

Associated data

  • GENBANK/U25746