ArticleProtein science : a publication of the Protein Society2009
The oligomerization of OxyR in Escherichia coli.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 7 citations in OpenAlex.
- Article
- Lifestyle-specific S-nitrosylation of protein cysteine thiols regulates Escherichia coli biofilm formation and resistance to oxidative stress.NPJ biofilms and microbiomes · 2021Article
- The Salmonella enterica serovar Typhi LeuO global regulator forms tetramers: residues involved in oligomerization, DNA binding, and transcriptional regulation.Journal of bacteriology · 2014Article
- Isolation and characterization of mutant Sinorhizobium meliloti NodD1 proteins with altered responses to luteolin.Journal of bacteriology · 2013Article
- Ultrasensitive response motifs: basic amplifiers in molecular signalling networks.Open biology · 2013Review
- ATP-dependent RecG helicase is required for the transcriptional regulator OxyR function in Pseudomonas species.The Journal of biological chemistry · 2012Article
- Haemophilus influenzae OxyR: characterization of its regulation, regulon and role in fitness.PloS one · 2012Article
- Article
- Establishing and maintaining sequestration of Dam target sites for phase variation of agn43 in Escherichia coli.Journal of bacteriology · 2010Article
- The oligomerization of CynR in Escherichia coli.Protein science : a publication of the Protein Society · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 lambdacI 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.