RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing

Hum Mol Genet. 2000 Mar 22;9(5):685-94. doi: 10.1093/hmg/9.5.685.


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 Tra2beta, an activator of pre-mRNA splicing that is ubiquitous but highly expressed in testis. Endogenous hnRNP G and Tra2beta proteins are associated in HeLa nuclear extracts. RBM and Tra2beta 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 Tra2beta. 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 Tra2beta-dependent splicing in spermatocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Drosophila Proteins*
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Humans
  • Male
  • Nuclear Proteins
  • RNA Splicing*
  • RNA-Binding Proteins / metabolism*
  • Ribonucleoproteins / metabolism*
  • Spermatogenesis*
  • Testis / metabolism
  • Two-Hybrid System Techniques
  • Y Chromosome*


  • Drosophila Proteins
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Nuclear Proteins
  • RBMY1A1 protein, human
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • tra2 protein, Drosophila