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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1997-5-9
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pubmed:abstractText |
In oocytes, nontranslated maternal mRNAs are packaged by protein into messenger ribonucleoprotein particles (mRNPs) that are masked from translation by protein-RNA interactions. Proteins associated with such masked states of mRNAs are particularly abundant in amphibian oocytes. One of these mRNP proteins from Xenopus oocytes, mRNP3+4 (also called FRG Y2a/b or p54/p56), binds to diverse mRNAs independent of their sequence and is the germ line member of the evolutionarily conserved Y box protein multigene family. Xenopus oocytes contain soluble pools of mRNP3+4 6 S oligomers, probably dimers, and larger approximately 15 S particles containing mRNP3+4 and additional proteins. Here we report the purification of this larger form as an approximately 320-kDa particle that contains mRNP3+4 and nine additional polypeptides, including mRNA-binding polypeptides of 34 and 36 kDa and a doublet of 110/105 kDa that proved to be nucleolin. The particle has a protein kinase activity that phosphorylates its own mRNP3+4, nucleolin, and a 31-kDa polypeptide component and exhibits translational inhibition in both the wheat germ extract and rabbit reticulocyte lysate systems. The presence of mRNP3+4 and nucleolin in this large translation regulatory particle suggests that it participates in an early step of mRNP assembly and masking.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/FRGY2 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nucleolin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10870-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9099743-Animals,
pubmed-meshheading:9099743-Chromatography, Gel,
pubmed-meshheading:9099743-Chromatography, Ion Exchange,
pubmed-meshheading:9099743-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9099743-Female,
pubmed-meshheading:9099743-Gene Expression Regulation,
pubmed-meshheading:9099743-Molecular Weight,
pubmed-meshheading:9099743-Multigene Family,
pubmed-meshheading:9099743-Nuclear Proteins,
pubmed-meshheading:9099743-Oocytes,
pubmed-meshheading:9099743-Phosphoproteins,
pubmed-meshheading:9099743-Protein Biosynthesis,
pubmed-meshheading:9099743-RNA, Messenger,
pubmed-meshheading:9099743-RNA-Binding Proteins,
pubmed-meshheading:9099743-Rabbits,
pubmed-meshheading:9099743-Reticulocytes,
pubmed-meshheading:9099743-Transcription Factors,
pubmed-meshheading:9099743-Xenopus Proteins,
pubmed-meshheading:9099743-Xenopus laevis
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pubmed:year |
1997
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pubmed:articleTitle |
A translation regulatory particle containing the Xenopus oocyte Y box protein mRNP3+4.
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pubmed:affiliation |
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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