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Murine Protein H is Comprised of 20 Repeating Units, 61 Amino Acids in Length
Torsten Kristensen and Brian F. Tack
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 11 (Jun. 1, 1986), pp. 3963-3967
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/27808
Page Count: 5
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A cDNA library constructed from size-selected (>28 S) poly(A)+ RNA isolated from the livers of C57B10.WR mice was screened by using a 249-base-pair (bp) cDNA fragment encoding 83 amino acid residues of human protein H as a probe. Of 120,000 transformants screened, 30 hybridized with this cDNA probe. Ten positives were colonypurified, and the largest plasmid cDNA insert, MH8 (4.4 kb), was sequenced by the dideoxy chain termination method. MH8 contained the complete coding sequence for the precursor of murine complement protein factor H (3702 bp), 100 bp of 5′-untranslated sequence, 448 bp of 3′-untranslated sequence, and a polyadenylylated tail of undetermined length. Murine pre-protein H was deduced to consist of an 18-amino acid signal peptide and 1216 residues of H-protein sequence. Murine H was composed of 20 repetitive units, each about 61 amino acid residues in length. Similar repetitive units are present in the C4b binding protein, the C3b-receptor (CR1), complement factor B and C2, and in β 2-glycoprotein I and the interleukin 2 receptor. This finding suggests a common evolutionary origin for regions of these proteins.
Proceedings of the National Academy of Sciences of the United States of America © 1986 National Academy of Sciences