HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Lamb, R. A. Search for Related Content PubMed PubMed Citation Articles by Lamb, R. A. Agricola Articles by Lamb, R. A.

The Phosphorylation of Sendai Virus Proteins by a Virus Particle-associated Protein Kinase

Department of Pathology, University of Cambridge Division of Virology, Laboratories Block, Addenbrookes' Hospital, Hills Road, Cambridge CB2 2QQ, U.K.

Highly purified Sendai virus contained a protein kinase activity which catalysed the phosphorylation of endogenous polypeptides or exogenous protamine sulphate. The virus contained very low levels of phosphoprotein phosphatase activity. Polyacrylamide gel analysis of the reaction product indicated that the phosphorylation was specific for certain polypeptides and varied according to whether the virus was grown in eggs or in tissue culture. This variation was partially associated with the difference in the polypeptide pattern that occurred when the virus was grown in eggs or in tissue culture. Characterization of these phosphoproteins demonstrated that the phosphate was incorporated predominantly in a phosphoester linkage with threonine residues. Using a detergent and high salt solubilization procedure, the protein kinase activity was found associated within glycoprotein free virus particles but not with the nucleocapsid-associated polypeptides. In vivo phosphorylation occurred when Sendai virus was grown in eggs or in tissue culture with [³²P] and the phosphorylated polypeptides were similar to those of the protein kinase reaction product. Phosphorylation could also be detected in the infected cell and could occur once the virus particle polypeptides were being synthesized. The non-structural polypeptides were not phosphorylated.

^* Present address: The Rockefeller University, New York, N.Y. 10021, U.S.A.

Received 17 June 1974; accepted 31 October 1974.

This article has been cited by other articles:

				C. Brownlee Inaugural Article: Biography of Robert A. Lamb PNAS, December 9, 2003; 100(25): 14607 - 14609. [Full Text] [PDF]

				T. Takimoto, T. Bousse, E. C. Coronel, R. A. Scroggs, and A. Portner Cytoplasmic Domain of Sendai Virus HN Protein Contains a Specific Sequence Required for Its Incorporation into Virions J. Virol., December 1, 1998; 72(12): 9747 - 9754. [Abstract] [Full Text] [PDF]