ArticleThe oligomerization of OxyR in Escherichia coli |
| Gwendowlyn S. Knapp 1 a, Jerry W. Tsai 1 2 b, James C. Hu 1 2 * |
1Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128
2Texas AgriLife Research, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128
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| email: James C. Hu (jimhu@tamu.edu) |
*Correspondence to James C. Hu, Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128
aCurrent address: Wadsworth Center, 120 New Scotland Avenue, PO Box 22002, Albany, New York 12201-2002
bCurrent address: Department of Chemistry, University of the Pacific, 3601 Pacific Avenue, Stockton, California
Funded by:
NIGMS (by Public Health Service); Grant Number: R01GM63652-01
| protein-protein interactions LysR-type transcriptional regulators OxyR oligomerization |
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  cI 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. |
Received: 21 July 2008; Revised: 25 September 2008; Accepted: 26 September 2008
10.1002/pro.5
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