Journal Article

RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2β and affect splicing

J.P. Venables, D.J. Elliott, O.V. Makarova, E.M. Makarov, H.J. Cooke and I.C. Eperon

in Human Molecular Genetics

Volume 9, issue 5, pages 685-694
Published in print March 2000 | ISSN: 0964-6906
Published online March 2000 | e-ISSN: 1460-2083 | DOI: http://dx.doi.org/10.1093/hmg/9.5.685
RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2β and affect splicing

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The RBMY gene family is found on the Y chromosome of all mammals, and microdeletions are strongly associated with infertility in men. RBMY expresses RBM only in the nuclei of germ cells, whereas its X chromosome homologue, RBMX, expresses hnRNP G ubiquitously. We show here that RBM, hnRNP G and a novel testis-specific relative, termed hnRNP G-T, interact with Tra2β, an activator of pre-mRNA splicing that is ubi­quitous but highly expressed in testis. Endogenous hnRNP G and Tra2β proteins are associated in HeLa nuclear extracts. RBM and Tra2β co-localize in two major domains in human spermatocyte nuclei. Phosphorylation enhanced the interaction and reduced competing RNA binding to the interaction domains. Incubation with the protein interaction domain of RBM inhibited splicing in vitro of a specific pre-mRNA substrate containing an essential enhancer bound by Tra2β. The RNA-binding domain of RBM affected 5′ splice site selection. We conclude that the hnRNP G family of proteins is involved in pre-mRNA splicing and infer that RBM may be involved in Tra2β-dependent splicing in spermatocytes.

Journal Article.  7848 words.  Illustrated.

Subjects: Genetics and Genomics

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