El Bounkari Omar, Guria Anuja, Klebba-Faerber Sabine, Claussen Maike, Pieler Tomas, Griffiths John R, Whetton Anthony D, Koch Alexandra, Tamura Teruko
Institut fuer Biochemie, OE4310 Medizinische Hochschule Hannover, Hannover, Germany.
FEBS Lett. 2009 Jan 5;583(1):13-8. doi: 10.1016/j.febslet.2008.11.024. Epub 2008 Dec 4.
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.
THOC7和Fms相互作用蛋白(FMIP)是与mRNA输出装置相关联的THO复合物的成员。FMIP是一种具有核定位信号(NLS)的核质穿梭蛋白,而THOC7不包含典型的NLS基序。我们在此表明,THOC7(氨基酸编号50 - 137)直接与FMIP的N端部分(1 - 199)结合。FMIP主要在细胞核中被检测到。在没有外源性FMIP的情况下,THOC7主要驻留在细胞质中,而在有FMIP的情况下,THOC7与FMIP一起被转运到细胞核中。此外,缺乏FMIP结合位点的THOC7不与FMIP共定位,这表明THOC7 / FMIP相互作用是THOC7核定位所必需的。