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Identification of a novel nuclear localization signal in Sam68
Author(s) -
Ishidate Takao,
Yoshihara Satoshi,
Kawasaki Yoshihiro,
Roy Badal Chandra,
Toyoshima Kumao,
Akiyama Tetsu
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00455-9
Subject(s) - nuclear localization sequence , nuclear transport , nuclear protein , tyrosine , sequence motif , peptide sequence , biology , rna , cell nucleus , rna binding protein , phosphorylation , biochemistry , nuclear export signal , nls , microbiology and biotechnology , fusion protein , nucleus , dna , transcription factor , gene , recombinant dna
Sam68, a nuclear RNA binding protein, binds to Src and is phosphorylated at tyrosine residues in an M‐phase specific manner. Here we identified a stretch of 24 amino acid residues in the COOH‐terminal portion of Sam68 which function as a nuclear localization signal. This signal sequence bears no apparent homology to any other known nuclear localization sequence. However, this sequence was found to contain a motif, PPXXR (P, Pro; R, Arg), which is conserved in various RNA binding proteins including hnRNP proteins. Replacement of Arg in this motif with Ala abolished the nuclear accumulation of a GFP fusion protein, suggesting that this residue is important in translocating the protein to the nucleus.