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The oligomerization of OxyR in Escherichia coli
Author(s) -
Knapp Gwendowlyn S.,
Tsai Jerry W.,
Hu James C.
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5
Subject(s) - repressor , mutant , mutagenesis , dimer , escherichia coli , alanine scanning , alanine , chemistry , regulator , biology , biochemistry , gene , amino acid , transcription factor , organic chemistry
We examine the contribution of residues at the dimer interface of the transcriptional regulator OxyR to oligomerization. Residues in contact across the dimer interface of OxyR were identified using the program Quaternary Contacts (QContacts). Site‐directed mutagenesis was performed on the non‐alanine or glycine residues identified in the resultant contact profile and the oligomerization ability of the mutant proteins was tested using the λcI repressor system to identify residues that are hot spots in OxyR. We compared the properties of these hot spots to those described in the literature from other systems. The hot spots identified in this study are not especially conserved amongst a set of OxyR orthologs.