1887

Abstract

Phosphoprotein patterns in two mutants of (ts) and (ts) , were analysed by two-dimensional polyacrylamide gel electrophoresis. Comparison with the phosphoprotein patterns of the mutants (ts) and , analysed in a previous study, demonstrated not only that the gene product is a positive element in the regulation of adenylyl cyclase activity, as suggested by recent studies, but that it is also a negative element in the phosphorylation of a 31 kDa protein (p31c and p31d), a protein whose phosphorylation is correlated with cell cycle arrest, and dephosphorylation with cell cycle initiation, respectively. Moreover, the phosphorylation phenotype of p31c and p31d suggests that the activity of the protein is subject to feedback regulation by cAMP-dependent protein kinase, and that the protein is a key element in an ammonium (NH ) signal-response system.

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1988-09-01
2021-10-19
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