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Isolation and Characterization of a Xenopus laevis C Protein cDNA: Structure and Expression of a Heterogeneous Nuclear Ribonucleoprotein Core Protein

Preugschat, Frank and Wold, Barbara J. (1988) Isolation and Characterization of a Xenopus laevis C Protein cDNA: Structure and Expression of a Heterogeneous Nuclear Ribonucleoprotein Core Protein. Proceedings of the National Academy of Sciences of the United States of America, 85 (24). pp. 9669-9673. ISSN 0027-8424. PMCID PMC282832. doi:10.1073/pnas.85.24.9669.

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The C proteins are major components of heterogeneous nuclear ribonucleoprotein complexes in nuclei of vertebrate cells. To begin to describe their structure, expression, and function we isolated and determined the DNA sequence of Xenopus laevis C protein cDNA clones. The protein predicted from the DNA sequence has a molecular mass of 30,916 kDa and is very similar to its human counterpart. Although mammalian genomes contain many copies of C protein sequence, the Xenopus genome contains few copies. When C protein RNA was synthesized in vitro and microinjected into stage-VI Xenopus oocytes, newly synthesized C proteins were efficiently localized in the nucleus. In vitro rabbit reticulocyte lysate and in vivo Xenopus oocyte translation systems both produce from a single mRNA two discrete polypeptide species that accumulate in a ratio similar to that of mammalian C1 and C2 proteins in vivo.

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Wold, Barbara J.0000-0003-3235-8130
Additional Information:© 1988 by the National Academy of Sciences Communicated by John Abelson, May 31, 1988. The sequence reported in this paper is being deposited in the EMBL/GenBank data base (IntelliGenetics, Mountain View, CA, and Eur. Mol. Biol. Lab., Heidelberg) (accession no. J03831). This work was supported by a Postgraduate Fellowship from the National Research Council of Canada (National Sciences and Engineering Research Council) and the Gordon Ross Fund to F.P. and grants from the National Institutes of Health and Rita Allen Foundation to B.W. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
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Natural Sciences and Engineering Research Council of Canada (NSERC)UNSPECIFIED
Gordon Ross Medical FoundationUNSPECIFIED
Rita Allen FoundationUNSPECIFIED
Issue or Number:24
PubMed Central ID:PMC282832
Record Number:CaltechAUTHORS:PREpnas88
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:702
Deposited By: Archive Administrator
Deposited On:15 Sep 2005
Last Modified:08 Nov 2021 19:04

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