Differential RNA-binding activity of the hnRNP G protein correlated with the sex genotype in the amphibian oocyte

Nucleic Acids Res. 2011 May;39(10):4109-21. doi: 10.1093/nar/gkq1315. Epub 2011 Jan 29.

Abstract

A proteomic approach has enabled the identification of an orthologue of the splicing factor hnRNP G in the amphibians Xenopus tropicalis, Ambystoma mexicanum, Notophthalmus viridescens and Pleurodeles walt, which shows a specific RNA-binding affinity similar to that of the human hnRN G protein. Three isoforms of this protein with a differential binding affinity for a specific RNA probe were identified in the P. walt oocyte. In situ hybridization to lampbrush chromosomes of P. waltl revealed the presence of a family of hnRNP G genes, which were mapped on the Z and W chromosomes and one autosome. This indicates that the isoforms identified in this study are possibly encoded by a gene family linked to the evolution of sex chromosomes similarly to the hnRNP G/RBMX gene family in mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amphibian Proteins / chemistry
  • Amphibian Proteins / genetics
  • Amphibian Proteins / metabolism*
  • Animals
  • Female
  • Genotype
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H / chemistry
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H / genetics
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H / metabolism*
  • Heterogeneous-Nuclear Ribonucleoproteins / chemistry
  • Humans
  • Multigene Family
  • Oocytes / metabolism
  • Peptides / chemistry
  • Peptides / metabolism
  • Pleurodeles / genetics
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • RNA Probes
  • Sex Chromosomes

Substances

  • Amphibian Proteins
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Peptides
  • Protein Isoforms
  • RBMX protein, human
  • RNA Probes