Literature DB >> 8505341

A mouse Y box protein, MSY1, is associated with paternal mRNA in spermatocytes.

S R Tafuri1, M Familari, A P Wolffe.   

Abstract

We have isolated a mouse cDNA clone, which encodes the protein MSY1 (mouse Y box protein 1), a new member of the Y box family of proteins. Northern analysis indicates that MSY1 mRNA accumulates over 100-fold more in testis than in other tissues. Moreover, MSY1 mRNA is developmentally regulated, initially appearing at the pachytene stage of spermatogenesis. This is the stage of maximal transcription and translation in the spermatocyte. In Xenopus laevis, homologous Y box proteins, FRGY1 and FRGY2, positively regulate transcription from promoters containing a Y box (CTGATTGGCCAA). In addition, the germ cell-specific Y box protein FRGY2 binds maternal mRNA within 60-80 S mRNP storage particles and in doing so regulates translation in the developing oocyte and embryo (Smith, L. D., Richter, J. D., and Taylor, M. A. (1984) in Molecular Biology of Development (Davidson, E. R., and Firtel, R. A., eds) pp. 129-141, Alan R. Liss, New York). The MSY1 protein can be isolated from a 60-80 S mRNP fraction of testis which like the frog oocyte contains stored, untranslated mRNAs. Furthermore, cross-linking experiments demonstrate that MSY1 is bound to mRNAs of this fraction. Finally, mobility shift analysis performed using the isolated protein indicates that MSY1 has nucleic acid binding properties similar to those of the FRGY proteins. These data suggest that the mouse Y box protein, MSY1, functions similarly to the FRGY2 protein in regulating the storage and translation of germ cell RNAs.

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Year:  1993        PMID: 8505341

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  29 in total

1.  Chicken Y-box proteins chk-YB-1b and chk-YB-2 repress translation by sequence-specific interaction with single-stranded RNA.

Authors:  S K Swamynathan; A Nambiar; R V Guntaka
Journal:  Biochem J       Date:  2000-06-01       Impact factor: 3.857

2.  Sequence-independent assembly of spermatid mRNAs into messenger ribonucleoprotein particles.

Authors:  E E Schmidt; E S Hanson; M R Capecchi
Journal:  Mol Cell Biol       Date:  1999-05       Impact factor: 4.272

3.  An acidic protein, YBAP1, mediates the release of YB-1 from mRNA and relieves the translational repression activity of YB-1.

Authors:  Ken Matsumoto; Kimio J Tanaka; Masafumi Tsujimoto
Journal:  Mol Cell Biol       Date:  2005-03       Impact factor: 4.272

4.  Human testis expresses a specific poly(A)-binding protein.

Authors:  C Féral; G Guellaën; A Pawlak
Journal:  Nucleic Acids Res       Date:  2001-05-01       Impact factor: 16.971

5.  Nucleic acid binding and intracellular localization of unr, a protein with five cold shock domains.

Authors:  H Jacquemin-Sablon; G Triqueneaux; S Deschamps; M le Maire; J Doniger; F Dautry
Journal:  Nucleic Acids Res       Date:  1994-07-11       Impact factor: 16.971

6.  Translation of a testis-specific Cu/Zn superoxide dismutase (SOD-1) mRNA is regulated by a 65-kilodalton protein which binds to its 5' untranslated region.

Authors:  W Gu; N R Hecht
Journal:  Mol Cell Biol       Date:  1996-08       Impact factor: 4.272

Review 7.  Transcription and masking of mRNA in germ cells: involvement of Y-box proteins.

Authors:  J Sommerville; M Ladomery
Journal:  Chromosoma       Date:  1996-04       Impact factor: 4.316

8.  Chicken YB-2, a Y-box protein, is a potent activator of Rous sarcoma virus long terminal repeat-driven transcription in avian fibroblasts.

Authors:  S K Swamynathan; A Nambiar; R V Guntaka
Journal:  J Virol       Date:  1997-04       Impact factor: 5.103

9.  Crystal structure of CspA, the major cold shock protein of Escherichia coli.

Authors:  H Schindelin; W Jiang; M Inouye; U Heinemann
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-24       Impact factor: 11.205

10.  Chicken MAR binding protein p120 is identical to human heterogeneous nuclear ribonucleoprotein (hnRNP) U.

Authors:  J P von Kries; F Buck; W H Strätling
Journal:  Nucleic Acids Res       Date:  1994-04-11       Impact factor: 16.971

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