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• W1803669888 endingPage "3728" @default.
• W1803669888 startingPage "3721" @default.
• W1803669888 abstract "We recently developed a simple technique for the generation of relatively large (31-codon) insertion mutations in cloned genes. To test whether the analysis of such mutations could provide insight into structure-function relationships in proteins, we examined a set of insertion mutants of the Escherichia coli lac repressor (LacI). Representatives of several LacI mutant classes were recovered, including mutants which exhibit fully active, inducer-insensitive, or weak dominant-negative phenotypes. The various properties of the recovered mutants agree with previous biophysical, biochemical, and genetic data for the protein. In particular, the results support the prior designation of mutationally tolerant spacer regions of LacI as well as proposed differences in dimerization interactions among regions of the protein core domain. These findings suggest that the analysis of 31-codon insertion mutations may provide a simple approach for characterizing structure-function relationships in proteins for which high-resolution structures are not available." @default.
• W1803669888 created "2016-06-24" @default.
• W1803669888 creator A5014003771 @default.
• W1803669888 creator A5060454508 @default.
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• W1803669888 date "1997-06-01" @default.
• W1803669888 modified "2023-10-15" @default.
• W1803669888 title "Insertion mutagenesis of the lac repressor and its implications for structure-function analysis" @default.
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• W1803669888 doi "https://doi.org/10.1128/jb.179.11.3721-3728.1997" @default.
• W1803669888 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/179170" @default.
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