Structural similarities of proteins encoded by three classes of avian sarcoma viruses

Neil, J. C. , Ghysdael, J., Smart, J. E. and Vogt, P. K. (1982) Structural similarities of proteins encoded by three classes of avian sarcoma viruses. Virology, 121(2), pp. 274-287. (doi: 10.1016/0042-6822(82)90167-2) (PMID:6289517)

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The structure and location of the phosphorylation sites of a number of avian sarcoma virus polyproteins have been examined by protease cleavage analysis. The PRCIIp and PRCII polyproteins, P170gag-fps and P105gag-fps yield indistinguishable cleavage fragments from an N-terminal region of 65,000 molecular weight, including the gag/non-gagjunction. This provides strong support for the view that PRCII arose directly from PRCIIp by a genomic deletion. For P909agag-yes, P800gag-yes, and P105gag-fps the major tyrosine phosphorylation sites are on C-terminal fragments of 27,000, 26,500, and 36,000 molecular weight, respectively. Further similarities have been shown by partial sequence analysis of the tyrosine phosphorylation sites; the positions of trypsin and staphylococcal V8 protease cleavage sites largely correspond in the src, fps, and yes gene products. The homology between the src and yes products is particularly striking. They yield C-terminal V8-resistant fragments of similar size, containing the major tyrosine phosphorylation sites which are indistinguishable after further cleavage with several proteases. These results suggest structural and functional relatedness between the src, fps, and yes gene products despite the lack of hybridization between their DNA sequences.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Neil, Professor James
Authors: Neil, J. C., Ghysdael, J., Smart, J. E., and Vogt, P. K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Virology
ISSN (Online):1096-0341
Published Online:10 February 2004

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