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Nucleic Acids Research, 1990, Vol. 18, No. 24 7331-7337
© 1990

Articles

Phosphorylation influences the binding of the yeast RAP1 protein to the upstream activating sequence of the PGK gene

Jimmy S.H. Tsang, Yves A.L. Henry, Alistair Chambers, Alan J. Kingsman1 and Susan M. Kingsman*

Department of Biochemistry, University of Oxford South Parks Road, Oxford, OX1 3QU 1Department of Molecular Biology, British Biotechnology Ltd Watlington Road, Cowley, Oxford, OX4 5LY, UK

*To whom correspondence should be addressed

Received September 6, 1990. Revised November 16, 1990. Accepted November 16, 1990.

Yeast repressor activator protein 1 (RAP 1) binds in vitro to specific DNA sequences that are found in diverse genetic elements. Expression of the yeast phosphoglycerate kinase gene (PGK) requires the binding of RAP1 to the activator core sequence within the upstream activating sequence (UAS) of PGK. A DNA fragment Z+ which contains the activator core sequence of the PGKUAS has been shown to bind RAP1. Here we report that phosphatase treatment of RAP1 affected its binding to the PGKUAS but that this depended on the nature of the sequence flanking the 5' end of the activator core sequence. When the sequence flanking the 5' end of the activator core sequence was different from the PGK RAP1-binding site, phosphatase treatment of RAP1 decreased its binding to the DNA. When the 5' end of the binding site was a match to the PGK RAP1-binding site dephosphorylation of RAP1 increased RAP1 binding to the DNA. These observations were reproduced when the minimal functional DNA-binding domain of the RAP1 protein was used, implicating a phosphorytation-dependent binding of RAP1. This is the first evidence for phosphorylation-dependent binding of RAP1.


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