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Science 30 March 1979:
Vol. 203. no. 4387, pp. 1346 - 1348
DOI: 10.1126/science.218289
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Articles

Science, Vol 203, Issue 4387, 1346-1348
Copyright © 1979 by American Association for the Advancement of Science

articles

Amino acid sequence homology between histone H5 and murine leukemia virus phosphoprotein p12

LE Henderson, RV Gilden, and S Oroszlan

The amino terminal acid sequences of several mouse leukemia virus phosphoproteins (p12) show definite homology with the amino terminal conserved region of H5 histones, the phosphorylated nuclear proteins of nucleated erythrocytes. Differences in the amino acid compositions of the two groups of proteins seem to rule out the possibility that they evolved from a single common ancestral gene. The finding of sequence homology between viral p12's and cellular histones, however, is consistent with evolution of retrovirus structural proteins by a process of differentiation from preexisting cellular genes. The conserved primary and secondary structure at the amino terminal region, common to both groups of proteins, may be related to their common function of nucleic acid binding modulated by phosphorylation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Phosphorylated Serine Residues and an Arginine-Rich Domain of the Moloney Murine Leukemia Virus p12 Protein Are Required for Early Events of Viral Infection.
A. Yueh and S. P. Goff (2003)
J. Virol. 77, 1820-1829
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