Nucleic Acids Research, 1994, Vol. 22, No. 12 2334-2343
© 1994
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GRSF-1: a poly(A)+ mRNA binding protein which interacts with a conserved G-rich element
Department of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School and Graduate School of Biomedical Sciences South Orange Avenue, Newark, NJ 07103, USA
*To whom correspondence should be addressed
Received March 7, 1994. Revised May 16, 1994. Accepted May 16, 1994.
Computer predictions identified similarities to a 14-base G-rich element in numerous mRNAs at a variety of locations. A Northwestern screening strategy was used to obtain a cDNA clone from a HeLa cell library using the G-rich RNA element as a probe. A cellular protein (called GRSF-1), which was encoded by this cDNA, binds RNAs containing the G-rich element. GRSF-1 was distinct from DSEF-1, a nuclear protein we have previously identified that interacts with the G-rich element, based on differences in molecular weight and partial peptide maps, as well as the lack of cross-reactivity with GRSF-1 specific monoclonal antibodies. Using indirect immunofluorescence microscopy, we localized GRSF-1 to the cytoplasm. In vivo UV cross-linking further demonstrated that GRSF-1 was bound to poly(A)+ mRNA in living human cells. Western blot analysis revealed four cytoplasmic proteins which expressed GRSF-1 specific epitopes. GRSF-1 contains three potential RNA recognition motifs and two auxiliary domains. Curiously, the domain organization of GRSF-1 is similar to the RNA binding proteins PUB1, ELAV, HuD, Hel-N1, mcs94-1 and RBP9.
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