| Literature DB >> 19059247 |
Omar El Bounkari1, Anuja Guria, Sabine Klebba-Faerber, Maike Claussen, Tomas Pieler, John R Griffiths, Anthony D Whetton, Alexandra Koch, Teruko Tamura.
Abstract
THOC7 and Fms-interacting protein (FMIP) are members of the THO complex that associate with the mRNA export apparatus. FMIP is a nucleocytoplasmic shuttling protein with a nuclear localization signal (NLS), whereas THOC7 does not contain a typical NLS motif. We show here that THOC7 (50-137, amino acid numbers) binds to the N-terminal portion (1-199) of FMIP directly. FMIP is detected mainly in the nucleus. In the absence of exogenous FMIP, THOC7 resides mainly in the cytoplasm, while in the presence of FMIP, THOC7 is transported into the nucleus with FMIP. Furthermore, THOC7 lacking the FMIP binding site does not co-localize with FMIP, indicating that THOC7/FMIP interaction is required for nuclear localization of THOC7.Entities:
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Year: 2008 PMID: 19059247 DOI: 10.1016/j.febslet.2008.11.024
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124