Nucleic Acids Research, 1984, Vol. 12, No. 6 2969-2985
© 1984
MOLECULAR BIOLOGY |
The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region
Biophysics Laboratory of the Graduate School, University of Wisconsin Madison, WI 53706 +Molecular Genetics, Inc. 10320 Bren Road East, Minnetonka, MN 55343, USA
*To whom reprint requests should be sent
Received December 19, 1983. Revised February 27, 1984. Accepted February 27, 1984.
The nucleotide sequence of 7200 bases of encephalomyocarditis (EMC) viral RNA, including the complete polyprotein-coding region, was determined. The polyprotein is encoded within a unique translational reading frame, 6870 bases in length. Protein synthesis begins with the sequence Met-Ala-Thr, and ends with the sequence Leu-Phe-Trp, 126 bases from the 3' end of the RNA. Viral capsid and noncapsid proteins were aligned with the deduced amino acid sequence of the polyprotein. The proteolytic processing map follows the standard 4-3-4 picornaviral pattern except for a short leader peptide (8 kd), which precedes the capsid proteins. Identification of the proteolytic cleavage sites showed that EMC viral protease, p22, has cleavage specificity for gln-gly or gln-ser sequences with adjacent proline residues. The cleavage specificity of the host-coded protease(s) includes both tyr-pro and gln-gly sequences.
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