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Lookup NU author(s): Professor David Elliott
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Almost every protein-coding gene undergoes pre-mRNA splicing, and the majority of these pre-mRNAs are alternatively spliced. Alternative exon usage is regulated by the transient formation of protein complexes on the pre-mRNA that typically contain heterogeneous nuclear ribonucleoproteins (hnRNPs). Here we characterize hnRNP G, a member of the hnRNP class of proteins. We show that hnRNP G is a nuclear protein that is expressed in different concentrations in various tissues and that interacts with other splicing regulatory proteins. hnRNP G is part of the supraspliceosome, where it regulates alternative splice site selection in a concentration-dependent manner. Its action on alternative exons can occur without a functional RNA-recognition motif by binding to other splicing regulatory proteins. The RNA-recognition motif of hnRNP G binds to a loose consensus sequence containing a CC(A/C) motif, and hnRNP G preferentially regulates alternative exons where this motif is clustered in close proximity. The X-chromosomally encoded hnRNP G regulates different RNAs than its Y-chromosomal paralogue RNA-binding motif protein, Y-linked (RBMY), suggesting that differences in alternative splicing, evoked by the sex-specific expression of hnRNP G and RBMY, could contribute to molecular sex differences in mammals. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Author(s): Heinrich B, Zhang Z, Raitskin O, Hiller M, Benderska N, Hartmann A, Bracco L, Elliott D, Ben-Ari S, Soreq H, Sperling J, Sperling R, Stamm S
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2009
Volume: 284
Issue: 21
Pages: 14303-14315
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
URL: http://dx.doi.org/10.1074/jbc.M901026200
DOI: 10.1074/jbc.M901026200
PubMed id: 19282290
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