Nucleic Acids Research, 1994, Vol. 22, No. 6 1059-1067
© 1994
MOLECULAR BIOLOGY |
The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization
Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine Philadelphia, PA 19104-6148, USA
*To whom correspondence should be addressed
Received November 23, 1993. Revised February 2, 1994. Accepted February 2, 1994.
More than 20 different heterogeneous nuclear ribo-nucleoprotelns (hnRNPs) are associated with pre-mRNAs in the nucleus of mammalian cells and these proteins appear to Influence pre-mRNA processing and other aspects of mRNA metabolism and transport. The arrangement of hnRNP proteins on pre-mRNAs is likely to be unique for each RNA and may be determined by the different RNA-bindlng preferences of each of these proteins. hnRNP F (Mr = 53 kD, pi = 6.1) and hnRNP H (Mr = 56 kD, pi = 6.7–7.1) are abundant components of immunopurifled hnRNP complexes and they have distinct nucleic acid binding properties. Unlike other hnRNP proteins which display a varying range of affinities for different ribonucleotidehomo polymers and ssDNA, hnRNP F and hnRNP H bind only to poly(rG) in vitro. hnRNP F and hnRNP H were purified from HeLa cells by poly(rG) affinity chromatography and oligonucleotldes derived from peptlde sequences were used to isolate a cDNA encoding hnRNP F. The predicted amlno acid sequence of hnRNP F revealed a novel protein with three repeated domains related to the RNP consensus sequence RNA-blndlng domain. Monoclonal antibodies produced against bacterially expressed hnRNP F were specific for both hnRNP F and hnRNP H and recognized related proteins In divergent organisms, including in the yeast Saccharomyces cerevlslae. hnRNP F and hnRNP H are thus highly related immunologically and they share identical peptldes. Interestingly, immunofluorescence microscopy revealed that hnRNP F and hnRNP H are concentrated in discrete regions of the nucleoplasm, in contrast to the general nucleoplasmlc distribution of previously characterized hnRNP proteins. The unique RNA-binding properties, amino acid sequence and distinct intranuclear localization of hnRNP F and hnRNP H make them novel hnRNP proteins that are likely to be important for the processing of RNAs containing guanosine-rlch sequences.
+ Present address: Harvard Medical School, Department of Microbiology, Cambridge, MA, USA
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