Abstract
The DBP5 gene encodes a putative RNA helicase of unknown function in the yeast Saccharomyces cerevisiae. It is shown here that Dbp5p is an ATP-dependent RNA helicase required for polyadenylated [poly(A)+] RNA export. Surprisingly, Dbp5p is present predominantly, if not exclusively, in the cytoplasm, and is highly enriched around the nuclear envelope. This observation raises the possibility that Dbp5p may play a role in unloading or remodeling messenger RNA particles (mRNPs) upon arrival in the cytoplasm and in coupling mRNP export and translation. The functions of Dbp5p are likely to be conserved, since its potential homologues can be found in a variety of eukaryotic cells.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Cell Line
-
Cytoplasm / enzymology
-
Dictyostelium / enzymology
-
Drosophila / embryology
-
Drosophila / enzymology
-
Embryo, Nonmammalian / enzymology
-
Evolution, Molecular
-
Female
-
Genomic Library
-
Humans
-
Jurkat Cells
-
Mice
-
Molecular Sequence Data
-
Nuclear Envelope / enzymology
-
Oocytes / physiology
-
PC12 Cells
-
Phylogeny
-
RNA Helicases
-
RNA Nucleotidyltransferases / chemistry
-
RNA Nucleotidyltransferases / genetics*
-
RNA Nucleotidyltransferases / metabolism*
-
RNA, Messenger / metabolism*
-
Rats
-
Recombinant Proteins / metabolism
-
Saccharomyces cerevisiae / enzymology*
-
Schizosaccharomyces / enzymology*
-
Sequence Alignment
-
Sequence Homology, Amino Acid
-
Subcellular Fractions / enzymology
-
Xenopus
Substances
-
RNA, Messenger
-
Recombinant Proteins
-
RNA Nucleotidyltransferases
-
RNA Helicases