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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

ybx2-a  -  Y box binding protein 2

Xenopus laevis

Synonyms: contrin, csda, csda3, dbpc, frgy2, ...
 
 
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High impact information on FRGY2

  • A role for transcription and FRGY2 in masking maternal mRNA within Xenopus oocytes [1].
  • Thus, the role of FRGY2 in the transcription and storage of maternal mRNA is similar to that of the transcription factor TFIIIA in the transcription and storage of 5S rRNA from the oocyte type 5S rRNA genes [2].
  • Surprisingly, FRGY2 is not only found to direct the accumulation of mRNA from promoters containing binding sites for the protein but also to selectively repress translation of the same mRNA [2].
  • The specificity and affinity of binding are determined by an RNA sequence motif similar to that used by the Xenopus laevis translation repressor FRGY2, which is conserved to varying degrees in the LHCBM gene family [3].
  • The Y-box protein FRGY2 inhibits translation of histone H4 mRNA in vitro [4].
 

Biological context of FRGY2

  • Of these, Xp54, the mRNA-masking protein FRGY2 and its activating protein kinase CK2alpha, bind to nascent transcripts on chromosome loops, whereas an Xp54-associated factor, RapA/B, binds to the mRNP complex in the cytoplasm [5].
 

Associations of FRGY2 with chemical compounds

  • Translation can be activated by treating the oocytes with progesterone or by injecting antibodies that bind the FRGY2 class of messenger RNA binding proteins, p56 and p60, but these antibodies are only effective if delivered to the nucleus [6].
 

Other interactions of FRGY2

  • A comparative analysis of FRGY2 and nucleolin C-terminal domains has revealed common structural features representing the signature of a particular type of auxiliary domain, which has co-evolved with the CSD and the RRM [7].
 

Analytical, diagnostic and therapeutic context of FRGY2

  • However, microinjection of reconstituted mRNPs into Xenopus oocytes demonstrates that although translational repression occurs in the absence of consensus RNA binding sequences for FRGY2, the presence of FRGY2 recognition elements within mRNA potentiates translational repression [8].
  • Visualization of the FRGY2-mRNA complexes by electron microscopy reveals that FRGY2 packages mRNA into a compact RNP [9].
  • Immunoprecipitation of the RNA-binding proteins demonstrated that one is xCIRP2 and that the other contains FRGY2 [10].

References

  1. A role for transcription and FRGY2 in masking maternal mRNA within Xenopus oocytes. Bouvet, P., Wolffe, A.P. Cell (1994) [Pubmed]
  2. Masking mRNA from translation in somatic cells. Ranjan, M., Tafuri, S.R., Wolffe, A.P. Genes Dev. (1993) [Pubmed]
  3. NAB1 is an RNA binding protein involved in the light-regulated differential expression of the light-harvesting antenna of Chlamydomonas reinhardtii. Mussgnug, J.H., Wobbe, L., Elles, I., Claus, C., Hamilton, M., Fink, A., Kahmann, U., Kapazoglou, A., Mullineaux, C.W., Hippler, M., Nickelsen, J., Nixon, P.J., Kruse, O. Plant Cell (2005) [Pubmed]
  4. Regulated unmasking of in vivo synthesized maternal mRNA at oocyte maturation. A role for the chaperone nucleoplasmin. Meric, F., Matsumoto, K., Wolffe, A.P. J. Biol. Chem. (1997) [Pubmed]
  5. Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation. Weston, A., Sommerville, J. Nucleic Acids Res. (2006) [Pubmed]
  6. Intron-less RNA injected into the nucleus of Xenopus oocytes accesses a regulated translation control pathway. Braddock, M., Muckenthaler, M., White, M.R., Thorburn, A.M., Sommerville, J., Kingsman, A.J., Kingsman, S.M. Nucleic Acids Res. (1994) [Pubmed]
  7. RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins. Manival, X., Ghisolfi-Nieto, L., Joseph, G., Bouvet, P., Erard, M. Nucleic Acids Res. (2001) [Pubmed]
  8. Translational repression dependent on the interaction of the Xenopus Y-box protein FRGY2 with mRNA. Role of the cold shock domain, tail domain, and selective RNA sequence recognition. Matsumoto, K., Meric, F., Wolffe, A.P. J. Biol. Chem. (1996) [Pubmed]
  9. Visualization of the reconstituted FRGY2-mRNA complexes by electron microscopy. Matsumoto, K., Tanaka, K.J., Aoki, K., Sameshima, M., Tsujimoto, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  10. CIRP2, a major cytoplasmic RNA-binding protein in Xenopus oocytes. Matsumoto, K., Aoki, K., Dohmae, N., Takio, K., Tsujimoto, M. Nucleic Acids Res. (2000) [Pubmed]
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