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Nucleic Acids Research, 1988, Vol. 16, No. 17 8307-8321
© 1988


Articles

Human Ul snRNP-specific C protein: complete cDNA and protein sequence and identification of a multigene family in mammals

Peter T.G. Sillekens*, Ria P. Beijer, Winand J. Habets and Walther J. van Venrooij

Department of Biochemistry, University of Nijmegen St Adelbertusplein 1, PO Box 9101, 6500 HB Nijmegen, The Netherlands

*To whom correspondence should be addressed

Received June 28, 1988. Revised August 3, 1988. Accepted August 3, 1988.

A complementary DNA clone for the human U1 snRNP-specific C protein has been isolated. The nucleotide sequence of the 733 bp cDNA insert includes a 15 bp 5'-untranslated region, an open reading frame of 477 bp corresponding to 159 amino acids (Mr-17, 373 D), and a 223 bp 3'-untranslated region. The identity of the clone was confirmed by in vitro translation of hybrid-selected mRNA or an RNA transcript synthesized from the cDNA. The in vitro synthesized C protein has a slightly greater mobility on SDS-polyacrylamide gels, indicating that the in vivo product is post-translationally modified. The deduced primary structure contains a segment of high proline and methionine content. A region homologous to the RNP consensus sequence, found in the other two U1 snRNP-specific proteins 70K and A, is absent. Analysis of genomic DNA restriction enzyme digests shows hybridizing fragments in the genome of all vertebrate classes. The results are consistent with multicopy representation of the C protein gene in mammals, whereas in the other vertebrate classes the related protein seems to be encoded by a single-copy gene.


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