Urate-responsive MarR homologs from Burkholderia
1Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. agrove@lsu.edu
Molecular Biosystems
|August 24, 2010
Summary
Researchers identified a conserved genetic element in Burkholderia species, involving a regulator protein and an efflux pump. Urate was found to attenuate the regulator's DNA binding, suggesting a urate-sensing mechanism.
Area of Science:
- Microbiology and Molecular Biology
- Genomics and Transcriptional Regulation
Background:
- The genus Burkholderia encompasses significant human pathogens.
- A conserved genomic locus includes a MarR family regulator and a major facilitator transport protein (MFTP) efflux pump.
Purpose of the Study:
- To investigate the function and ligand-binding properties of a MarR homolog in Burkholderia.
- To determine if this regulator responds to urate and affects MFTP expression.
Main Methods:
- Homology modeling of the MarR homolog to identify conserved ligand-binding residues.
- Analysis of DNA binding specificity of the B. thailandensis MarR homolog.
- Testing the effect of urate, xanthine, hypoxanthine, adenine, and allantoin on DNA binding.
Main Results:
- The MarR homolog shares a four amino acid urate-binding signature with other homologs.
- Urate, xanthine, and hypoxanthine attenuated the regulator's specific DNA binding.
- Adenine and allantoin did not affect DNA binding.
Conclusions:
- A subset of MarR homologs possess a urate-binding signature, responding to urate by reduced DNA binding.
- The regulator likely controls the MFTP, suggesting a role in efflux pump regulation.
- The regulator was proposed to be named MftR (major facilitator transport regulator).
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