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Human Molecular Genetics, 2000, Vol. 9, No. 5 685-694
© 2000 Oxford University Press

RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2ß and affect splicing

J.P. Venables1,2, D.J. Elliott2, O.V. Makarova1,+, E.M. Makarov1,+, H.J. Cooke2 and I.C. Eperon1,§

1Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, UK and 2Medical Research Council Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK

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 Tra2ß, an activator of pre-mRNA splicing that is ubi­quitous but highly expressed in testis. Endogenous hnRNP G and Tra2ß proteins are associated in HeLa nuclear extracts. RBM and Tra2ß 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 Tra2ß. 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 Tra2ß-dependent splicing in spermatocytes.

+ Present address: Institut für Molekularbiologie und Tumorforschung, Philipps-Universität, Emil-Mannkopff-Strasse 2, D-35037, Marburg, Germany

§ To whom correspondence should be addressed. Tel: +44 116 2523482; Fax: +44 116 2523369; Email: eci@le.ac.uk


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