Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.
Authors:
- M H HechtMHM H Hecht
- H C NelsonHNH C Nelson
- R T SauerRSR T Sauer
- 1 May 1983
- journal article
- research article
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 80 (9) , 2676-2680
Abstract
The DNA binding properties of 52 different single-amino acid substitutions in lambda repressor's amino-terminal domain have been characterized. Seven proteins bearing mutations that change solvent-exposed side chains have been purified. The amino-terminal domains of these mutant repressors are folded and are comparable to the wild-type amino-terminal domain in thermal stability. In contrast, a purified mutant repressor bearing a substitution in a buried side chain contains an amino-terminal domain with decreased thermal stability. We argue that mutations that alter solvent-exposed wild-type side chains define residues that form the operator DNA binding surface of lambda repressor whereas completely or partially buried mutations exert their effect by decreasing protein stability.Keywords
This publication has 15 references indexed in Scilit:
- Gene regulation at the right operator (OR) of bacteriophage λJournal of Molecular Biology, 1980
- [76] Bacteriophage λ repressor and cro protein: Interactions with operator DNA1980
- [57] Sequencing end-labeled DNA with base-specific chemical cleavages1980
- How the λ repressor and cro workCell, 1980
- Regulatory functions of the λ repressor reside in the amino-terminal domainNature, 1979
- DNA sequence of the bacteriophage λ cI geneNature, 1978
- Primary structure of the λ repressorBiochemistry, 1978
- Maximizing gene expression on a plasmid using recombination in vitroCell, 1978
- [20] Applications of thermolysin in protein structural analysis1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970