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Volume 272, Number 16, Issue of April 18, 1997 pp. 10870-10876
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Translation Regulatory Particle Containing the Xenopus Oocyte Y Box Protein mRNP3+4

(Received for publication, September 23, 1996, and in revised form, January 29, 1997)

From the Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202

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 ~15 S particles containing mRNP3+4 and additional proteins. Here we report the purification of this larger form as an ~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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