Nucleic Acids Research, 1990, Vol. 18, No. 13 3871-3879
© 1990
MOLECULAR BIOLOGY |
Characterization of a human cDNA encoding a widely expressed and highly conserved cysteine-rich protein with an unusual zinc-finger motif
1Howard Hughes Medical Institute, University of Pennsylvania Philadelphia, PA 19104, USA 2Department of Human Genetics, University of Pennsylvania Philadelphia, PA 19104, USA 3Department of Medicine, University of Pennsylvania Philadelphia, PA 19104, USA 4Biology, University of Pennsylvania Philadelphia, PA 19104, USA
*To whom correspondence should be addressed at Howard Hughes Medical Institute, Department of Human Genetics, University of Pennsylvania School of Medicine, 422 Curie Boulevard, Philadelphia, PA 19104-6145, USA
Received March 27, 1990. Revised June 5, 1990. Accepted June 5, 1990.
A human term placental cDNA library was screened at low stringency with a human prolactin cDNA probe. One of the cDNAs isolated hybridizes to a 1.8 kb mRNA present in all four tissues of the placenta as well as to every nucleated tissue and cell line tested. The sequence of the full-length cDNA was determined. An extended open reading frame predicted an encoded protein product of 20.5 kDa. This was directly confirmed by the in vitro translation of a synthetic mRNA transcript. Based upon the characteristic placement of cysteine (C) and histidine (H) residues in the predicted protein structure, this molecule contains four putative zinc fingers. The first and third fingers are of the C4 class while the second and fourth are of the C2HC class. Based upon sequence similarities between the first two and last two zinc fingers and sequence similarities to a related rodent protein, cysteine-rich intestinal protein (CRIP), these four finger domains appear to have evolved by duplication of a preexisting two finger unit. Southern blot analyses indicate that this human cysteine-rich protein (hCRP) gene has been highly conserved over the span of evolution from yeast to man. The characteristics of this protein suggest that it serves a fundamental role in cellular function.
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