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Published December 15, 1988 | Published
Journal Article Open

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


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.

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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