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Nucleic Acids Research, 1990, Vol. 18, No. 2 291-298
© 1990

MOLECULAR BIOLOGY

Yeast regulatory protein LEU3: a structure-function analysis

Kemin Zhou, Yinglin Bai and Gunter B. Kohlhaw

Department of Biochemistry, Purdue University West Lafayette, IN 47907, USA

Received September 28, 1989. Revised December 8, 1989. Accepted December 8, 1989.

Eleven mutations resulting in partially deleted or truncated LEU3 protein were generated by linker insertion or other modifications at restriction sites, deletion of restriction fragments, or oligonucleotidedirected mutagenesis. Functional studies of these mutants showed the following: (i) A specific DNA binding region is contained within the 173 N-terminal residues, but other regions of the protein are required for optimal binding. (ii) Activation of LEU2 expression depends on the C-terminal 113 residues of the LEU3 protein. (iii) Deletion of part or all of a central section of LEU3 eliminates the ability of the LEU3 protein to respond to the co-activator {alpha}-isopropylmalate, i.e. creates an unmodulated activator. (iv) Overproduction of unmodulated activator slows down cell growth. (v) Specific deletion of two short acidic regions, including one with net charge –19, has only minor effects on activation and modulation.


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