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[The major cytoplasmic mRNP protein, p50, is required for efficient mRNA translation in vitro].

Authors
  • Kovrigina, E A
  • Nashchekin, D V
  • Evdokimova, V M
  • Ovchinnikov, L P
Type
Published Article
Journal
Biokhimii︠a︡ (Moscow, Russia)
Publication Date
Dec 01, 1996
Volume
61
Issue
12
Pages
2173–2180
Identifiers
PMID: 9156558
Source
Medline
License
Unknown

Abstract

The major cytoplasmic mRNP protein of somatic cells, p50, is the member of the Y-box-binding transcription factor family and can control gene expression at two levels including mRNA transcription and translation. It has been demonstrated that p50 is responsible for the inactive state of mRNA within free mRNPs. In this work, we show that the Y-box-containing DNA (Y-DNA) predominantly binds to p50 in rabbit reticulocyte lysates and causes translation inhibition of the endogenous and exogenous globin mRNA and prokaryotic beta-galactosidase mRNA. Preincubation of Y-DNA with purified p50 prevents the inhibition. Inhibition of protein biosynthesis by the Y-DNA is not due to the degradation or functional inactivation of mRNA. The inhibition is associated with the decay of polyribosomes and dissociation of a newly synthesized protein from the ribosomes. The data indicate that Y-DNA inhibits protein biosynthesis predominantly at the initiation stage and that p50 is an essential component of the translation initiation apparatus.

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