Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1997-5-9
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10870-6
pubmed:dateRevised
2006-11-15
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
pubmed:year
1997
pubmed:articleTitle
A translation regulatory particle containing the Xenopus oocyte Y box protein mRNP3+4.
pubmed:affiliation
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't