A cellular cofactor for the constitutive transport element of type D retrovirus.
A human nuclear protein that specifically interacts with the constitutive transport element (CTE) of simian retrovirus was identified as adenosine 5'-triphosphate-dependent RNA helicase A. This protein could bind to functional CTE but not to inactive CTE mutants. The interaction of helicase A with CTE was distinct from previously described helicase activity of this protein. Helicase A shuttled from the nucleus to the cytoplasm in the presence of a transcription inhibitor or in cells transiently overexpressing CTE-containing RNA. In vivo colocalization of helicase A and CTE was observed in experiments that combined in situ hybridization and immunostaining. These results suggest that helicase A plays a role in the nuclear export of CTE-containing RNA.
Tang
H
H
Department of Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Gaietta
G M
GM
Fischer
W H
WH
Ellisman
M H
MH
Wong-Staal
F
F
D000255:Adenosine Triphosphate / Q000378:metabolism; D030121:Betaretrovirus / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D002467:Cell Nucleus / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism*; D011485:Protein Binding; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000378:metabolism*; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism*
D009687:Nuclear Proteins; D012367:RNA, Viral; D000255:Adenosine Triphosphate; D012316:RNA Nucleotidyltransferases; D020365:RNA Helicases