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Title: Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos

Abstract

To gain insight into the mechanisms involved in the formation of maternally stored mRNPs during Xenopus laevis development, we searched for soluble cytoplasmic proteins of the oocyte that are able to selectively bind mRNAs, using as substrate radiolabeled mRNA. In vitro mRNP assembly in solution was followed by UV-cross-linking and RNase digestion, resulting in covalent tagging of polypeptides by nucleotide transfer. Five polypeptides of approximately 54, 56 60, 70, and 100 kD (p54, p56, p60, p70, and p100) have been found to selectively bind mRNA and assemble into mRNPs. These polypeptides, which correspond to previously described native mRNP components, occur in three different particle classes of approximately 4.5S, approximately 6S, and approximately 15S, as also determined by their reactions with antibodies against p54 and p56. Whereas the approximately 4.5S class contains p42, p60, and p70, probably each in the form of individual molecules or small complexes, the approximately 6S particles appears to consist only of p54 and p56, which occur in a near-stoichiometric ratio suggestive of a heterodimer complex. The approximately 15S particles contain, in addition to p54 and p56, p60 and p100 and this is the single occurring form of RNA-binding p100. We have also observed changes in themore » in vitro mRNA binding properties of these polypeptides during oogenesis and early embryonic development, in relation to their phosphorylation state and to the activity of an approximately 15S particle-associated protein kinase, suggesting that these proteins are involved in the developmental translational regulation of maternal mRNAs.« less

Authors:
; ;  [1]
  1. (Institute of Cell and Tumor Biology, Heidelberg (Germany, F.R.))
Publication Date:
OSTI Identifier:
5984745
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Cell Biology; (USA); Journal Volume: 112:1
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; FROGS; ONTOGENESIS; MESSENGER-RNA; BIOCHEMICAL REACTION KINETICS; POLYPEPTIDES; BIOSYNTHESIS; CROSS-LINKING; CYTOPLASM; EMBRYOS; NUCLEOPROTEINS; OOCYTES; PHOSPHORYLATION; PHOSPHOTRANSFERASES; RNA-ASE; ULTRAVIOLET RADIATION; AMPHIBIANS; ANIMALS; AQUATIC ORGANISMS; CELL CONSTITUENTS; CHEMICAL REACTIONS; ELECTROMAGNETIC RADIATION; ENZYMES; ESTERASES; GERM CELLS; HYDROLASES; KINETICS; NUCLEIC ACIDS; ORGANIC COMPOUNDS; PEPTIDES; PHOSPHODIESTERASES; PHOSPHORUS-GROUP TRANSFERASES; POLYMERIZATION; PROTEINS; RADIATIONS; REACTION KINETICS; RNA; SYNTHESIS; TRANSFERASES; VERTEBRATES; 560120* - Radiation Effects on Biochemicals, Cells, & Tissue Culture

Citation Formats

Murray, M.T., Krohne, G., and Franke, W.W. Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos. United States: N. p., 1991. Web. doi:10.1083/jcb.112.1.1.
Murray, M.T., Krohne, G., & Franke, W.W. Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos. United States. doi:10.1083/jcb.112.1.1.
Murray, M.T., Krohne, G., and Franke, W.W. Tue . "Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos". United States. doi:10.1083/jcb.112.1.1.
@article{osti_5984745,
title = {Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos},
author = {Murray, M.T. and Krohne, G. and Franke, W.W.},
abstractNote = {To gain insight into the mechanisms involved in the formation of maternally stored mRNPs during Xenopus laevis development, we searched for soluble cytoplasmic proteins of the oocyte that are able to selectively bind mRNAs, using as substrate radiolabeled mRNA. In vitro mRNP assembly in solution was followed by UV-cross-linking and RNase digestion, resulting in covalent tagging of polypeptides by nucleotide transfer. Five polypeptides of approximately 54, 56 60, 70, and 100 kD (p54, p56, p60, p70, and p100) have been found to selectively bind mRNA and assemble into mRNPs. These polypeptides, which correspond to previously described native mRNP components, occur in three different particle classes of approximately 4.5S, approximately 6S, and approximately 15S, as also determined by their reactions with antibodies against p54 and p56. Whereas the approximately 4.5S class contains p42, p60, and p70, probably each in the form of individual molecules or small complexes, the approximately 6S particles appears to consist only of p54 and p56, which occur in a near-stoichiometric ratio suggestive of a heterodimer complex. The approximately 15S particles contain, in addition to p54 and p56, p60 and p100 and this is the single occurring form of RNA-binding p100. We have also observed changes in the in vitro mRNA binding properties of these polypeptides during oogenesis and early embryonic development, in relation to their phosphorylation state and to the activity of an approximately 15S particle-associated protein kinase, suggesting that these proteins are involved in the developmental translational regulation of maternal mRNAs.},
doi = {10.1083/jcb.112.1.1},
journal = {Journal of Cell Biology; (USA)},
number = ,
volume = 112:1,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 1991},
month = {Tue Jan 01 00:00:00 EST 1991}
}