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Showing papers on "Protein–protein interaction published in 1982"


Journal ArticleDOI
TL;DR: Results indicated that specific interactions among the three proteins gp22, gp23, and gp24 may play a role in the regulation of T4 capsid-length determination.
Abstract: A bacteriophage T4 mutation (ptg19-80c) located in gene 23, which encodes the major structural protein of the T4 capsid, results in the production of capsids of abnormal length. Mutations outside gene 23 which partially suppress ptg19-80c have been described in the accompanying paper (D. H. Doherty, J. Virol. 43:641-654, 1982). Characterization of these suppressors was extended. A complementation test suggested that the suppressors were in genes 22 and 24. These genes coded for the major component of the morphogenetic core of the capsid precursor and the vertex protein of the capsid, respectively. The suppressor mutations were found to have no obvious phenotype in the absence of ptg19-80c. Suppression was shown to be allele specific: other ptg mutations at different sites in gene 23 were not suppressed by the suppressors of ptg19-80c. These results indicated that specific interactions among the three proteins gp22, gp23, and gp24 may play a role in the regulation of T4 capsid-length determination. Current models for capsid-length determination are considered in the light of these results.

13 citations


Journal ArticleDOI
TL;DR: Protein-protein interaction of Moloney murine leukaemia virus was studied by an assay where one protein preparation was coupled covalently to Sepharose, and binding of radiolabelled proteins to the protein-Sepharose was examined.
Abstract: Protein-protein interaction of Moloney murine leukaemia virus was studied by an assay where one protein preparation was coupled covalently to Sepharose, and binding of radiolabelled proteins to the protein-Sepharose was examined. It was found that the virus proteins gp70, p30, p15E and p15 in solution could associate weakly to disrupted virus particles and to p30. However, when the disrupted virus particles and p30 were coupled to Sepharose in the presence of Triton X-100, stronger binding of the four proteins was observed. Only low or no binding of p12 and p10 was observed to these protein-Sepharoses. The results are discussed with respect to the assembly and structure of the virus particle.

3 citations