JBC, Vol. 250, Issue 16, 6232-6239, Aug, 1975
Amino acid sequence homology of mammalian type C RNA virus major internal proteins
S. Oroszlan, T. Copeland, M. R. Summers, G. Smythers and R. V. Gilden
The NH2-terminal amino acid sequence of the major group-specific antigen,
the major internal virion protein (p30; approximate molecular weight
30,000) of several mammalian type C RNA viruses was determined by the Edman
degradation procedure using an automated protein sequenator. All of the
proteins analyzed show a high degree of over-all sequence homology and also
contain specific regions or single residues. All p30s begin with the
sequence prolyl-leucylarginyl (Pro-Leu-Arg) and have an invariant,
conserved region from residues 11 to 24. In this region only a single amino
acid difference appears between the cat and mouse p30s. At position 17
alanine is found in the cat, and serine in all the mouse proteins. This
homologous region starts at position 10 for RD-114 and baboon virus p30s,
and at position 18 in the protein of the virus isolated from gibbon ape.
The region extending from residue 4 to 10 shows considerable variability
between p30s isolated from different mammalian species. Out of 24 residues
compared, only a single amino acid difference was found between six
different mouse p30s. At position 4, three have leucine, two have alanine,
and one has serine. The comparative sequence data demonstrate that the
viral p30s are products of related genes in the viruses from various
mammalian species.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
