An NH sub(2)-terminal peptide from the vaccinia virus L1R protein directs the myristylation and virion envelope localization of a heterologous fusion protein

• Published in: The Journal of biological chemistry Vol. 268; no. 10; pp. 7585 - 7593
• Main Authors: Ravanello, M P, Franke, CA, Hruby, DE
• Format: Journal Article
• Language: English
• Published: 01-01-1993
• Subjects: envelopes; fusion protein; L1R protein; myristylation; N-terminus; peptides; vaccinia virus; virions
• ISSN: 0021-9258

The vaccinia virus L1R gene product is a late protein destined for insertion into the envelope of intracellular virus particles. Because this protein is co-translationally modified by the addition of myristic acid to the penultimate NH sub(2)-terminal glycine residue, it was of interest to identify the modification signal within the L1R protein and to assess the relevance of myristylation to protein localization. A family of chimeric reporter genes containing 0-13 codons from the NH sub(2) terminus of the L1R open reading frame fused in-frame to the bacterial chloramphenicol acetyltransferase gene was constructed. The encoded proteins were tested as myristylation substrates in cell-free extracts and infected cells. The results obtained in vitro and in vivo were similar and suggested that although the NH sub(2)-terminal 5 amino acids of the L1R protein were the minimum signal required to observed modification by myristate, 12 amino acids were required to obtain wild type levels of myristylation with a modulating role played by the intervening amino acid residues.