Literature DB >> 6727992

Reversible inhibition of translation by Xenopus oocyte-specific proteins.

J D Richter, L D Smith.   

Abstract

A characteristic of growing oocytes of all animal species is the synthesis and accumulation of messenger RNA which is destined to be used primarily by the early embryo. The mechanism(s) which regulates the translation of this maternal mRNA remains unknown. However, the inability of the oocyte to translate all of its putative mRNA has been attributed to at least three limitations: (1) The rate of translation is limited by the availability of components of the translational apparatus other than mRNA, (2) the structural organization of the mRNA prevents translation, and (3) proteins associated with the mRNA prevent translation. Several investigators have suggested that proteins associated with maternal mRNA suppress translation in sea urchin eggs, although others claim that such results may be due to experimental artefacts. Oocyte-specific proteins have been identified in association with non-translating poly(A)+ mRNAs from Xenopus laevis oocytes, and we report here that when these proteins are reconstituted with mRNAs in vitro the translation of the mRNAs in vitro is reversibly repressed. The implication is that these proteins are involved in the regulation of translation of stored maternal mRNAs.

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Year:  1984        PMID: 6727992     DOI: 10.1038/309378a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  33 in total

1.  The major mRNA-associated protein YB-1 is a potent 5' cap-dependent mRNA stabilizer.

Authors:  V Evdokimova; P Ruzanov; H Imataka; B Raught; Y Svitkin; L P Ovchinnikov; N Sonenberg
Journal:  EMBO J       Date:  2001-10-01       Impact factor: 11.598

2.  Structural organization of mRNA complexes with major core mRNP protein YB-1.

Authors:  Maxim A Skabkin; Olga I Kiselyova; Konstantin G Chernov; Alexey V Sorokin; Evgeniy V Dubrovin; Igor V Yaminsky; Victor D Vasiliev; Lev P Ovchinnikov
Journal:  Nucleic Acids Res       Date:  2004-10-19       Impact factor: 16.971

3.  Akt-mediated YB-1 phosphorylation activates translation of silent mRNA species.

Authors:  Valentina Evdokimova; Peter Ruzanov; Michael S Anglesio; Alexey V Sorokin; Lev P Ovchinnikov; Jonathan Buckley; Timothy J Triche; Nahum Sonenberg; Poul H B Sorensen
Journal:  Mol Cell Biol       Date:  2006-01       Impact factor: 4.272

4.  Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins.

Authors:  M T Murray; D L Schiller; W W Franke
Journal:  Proc Natl Acad Sci U S A       Date:  1992-01-01       Impact factor: 11.205

5.  Cell-free translation systems prepared from starfish oocytes faithfully reflect in vivo activity; mRNA and initiation factors stimulate supernatants from immature oocytes.

Authors:  Z Xu; M B Hille
Journal:  Cell Regul       Date:  1990-12

6.  Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA.

Authors:  K Matsumoto; K M Wassarman; A P Wolffe
Journal:  EMBO J       Date:  1998-04-01       Impact factor: 11.598

7.  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

8.  Overexpression in COS cells of p50, the major core protein associated with mRNA, results in translation inhibition.

Authors:  E K Davydova; V M Evdokimova; L P Ovchinnikov; J W Hershey
Journal:  Nucleic Acids Res       Date:  1997-07-15       Impact factor: 16.971

9.  Xp54, the Xenopus homologue of human RNA helicase p54, is an integral component of stored mRNP particles in oocytes.

Authors:  M Ladomery; E Wade; J Sommerville
Journal:  Nucleic Acids Res       Date:  1997-03-01       Impact factor: 16.971

10.  Cap-independent translation initiation in Xenopus oocytes.

Authors:  B D Keiper; R E Rhoads
Journal:  Nucleic Acids Res       Date:  1997-01-15       Impact factor: 16.971

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