Evidence for an autoprotease activity of Sindbis virus capsid protein
G Aliperti, MJ Schlesinger - Virology, 1978 - Elsevier
G Aliperti, MJ Schlesinger
Virology, 1978•ElsevierSindbis virus capsid protein is virtually the only product formed when viral 26 S RNA is
added to a mouse Krebs ascites cell-free protein synthesis system. However, substitution of
arginine and proline by the respective analogues canavanine and azetidine-2-carboxylate
inhibits capsid production and larger polypeptides accumulate. The latter are converted to
capsid in pulse-chase experiments when the normal amino acids are added during the
chase, but not if the chase period contains only the analogues in the reaction mixture. These …
added to a mouse Krebs ascites cell-free protein synthesis system. However, substitution of
arginine and proline by the respective analogues canavanine and azetidine-2-carboxylate
inhibits capsid production and larger polypeptides accumulate. The latter are converted to
capsid in pulse-chase experiments when the normal amino acids are added during the
chase, but not if the chase period contains only the analogues in the reaction mixture. These …
Abstract
Sindbis virus capsid protein is virtually the only product formed when viral 26 S RNA is added to a mouse Krebs ascites cell-free protein synthesis system. However, substitution of arginine and proline by the respective analogues canavanine and azetidine-2-carboxylate inhibits capsid production and larger polypeptides accumulate. The latter are converted to capsid in pulse-chase experiments when the normal amino acids are added during the chase, but not if the chase period contains only the analogues in the reaction mixture. These results support an autoprotease model for the co-translational cleavage of Sindbis virus capsid proteins.
Elsevier
