Cleavage of four avian sarcoma virus polyproteins with virion protease p15 removes gag sequences and yields large fragments that function as tyrosine phosphoacceptors in vitro

Ghysdael, J., Neil, J.C. and Vogt, P.K. (1981) Cleavage of four avian sarcoma virus polyproteins with virion protease p15 removes gag sequences and yields large fragments that function as tyrosine phosphoacceptors in vitro. Proceedings of the National Academy of Sciences of the United States of America, 78(9), pp. 5847-5851. (PMID:6170987)

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Publisher's URL: http://www.jstor.org/stable/11566

Abstract

The transformation-specific polyproteins of avian sarcoma viruses PRCII, PRCII-p, Fujinami sarcoma virus (FSV), and Esh sarcoma virus (ESV) consist of two domains, one derived from a partial viral gag gene and the other representing an apparently cell-derived insert in the defective viral genome. These gag-linked proteins were cleaved with retrovirion protease p15. Cleavage of PRCII-p polyprotein P170, P105 of PRCII, and P140 of FSV occurred within the gag domain and generated fragments of Mr 130,000, 70,000, and 115,000, respectively, containing all of the transformation-specific sequences linked to a remnant of the original gag sequences. ESV P80 was cleaved inside the transformation-specific domain, yielding a Mr 35,000--38,000 fragment from the NH2-terminal half of the molecule consisting of the entire gag portion and some no-gag sequences and a Mr 48,000 fragment containing most of the transformation-specific sequences. The tyrosine phosphorylation sites of the polyproteins were found in every case in the transformation-specific fragments. The major serine phosphorylation site of ESV P80 was found to reside in the Mr 35,000--38,000 gag-containing fragment, probably within the transformation-specific sequences of that cleavage product. Removal of all of the gag domain of ESV P80 or most of the gag domain in PRCII-p P170, PRCII P105, and FSV P140 does not affect their ability to be phosphorylated by the polyprotein-associated tyrosine-specific protein kinase activities. This observation suggests that the gag sequences of the polyproteins of classes II (PRCII-p, PRCII, and FSV) and III (ESV) avian sarcoma viruses may not be required for this enzymatic function, which appears to be of importance in transformation.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Neil, Professor James
Authors: Ghysdael, J., Neil, J.C., and Vogt, P.K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Proceedings of the National Academy of Sciences of the United States of America
Publisher:National Academy of Sciences
ISSN:0027-8424

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