Mutations in λ repressor's amino-terminal domain: Implications for protein stability and DNA binding

M. H. Hecht, H. C.M. Nelson, R. T. Sauer

Research output: Contribution to journalArticlepeer-review

113 Scopus citations

Abstract

The DNA binding properties of 52 different single-amino acid substitutions in λ 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 λ repressor whereas completely or partially buried mutations exert their effect by decreasing protein stability.

Original languageEnglish (US)
Pages (from-to)2676-2680
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume80
Issue number9 I
DOIs
StatePublished - 1983

All Science Journal Classification (ASJC) codes

  • General

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