PMCCPMCCPMCC

Search tips
Search criteria 

Advanced

 
Logo of narLink to Publisher's site
 
Nucleic Acids Res. Jan 25, 1990; 18(2): 291–298.
PMCID: PMC330266
Yeast regulatory protein LEU3: a structure-function analysis.
K M Zhou, Y L Bai, and G B Kohlhaw
Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
Abstract
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 oligonucleotide-directed 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.
Full text
Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.6M), or click on a page image below to browse page by page.
Images in this article
Click on the image to see a larger version.
Articles from Nucleic Acids Research are provided here courtesy of
Oxford University Press