ArticleJournal of bacteriology2011
Promoter discrimination at class I MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Targeting MarA N-terminal domain dynamics to prevent DNA binding.Protein science : a publication of the Protein Society · 2025Article
- Physiological Effects of TolC-Dependent Multidrug Efflux Pumps in Escherichia coli: Impact on Motility and Growth Under Stress Conditions.MicrobiologyOpen · 2024Article
- Article
- Elucidation of Key Interactions between VirF and theJournal of bacteriology · 2022Article
- Acidification of Cytoplasm in Escherichia coli Provides a Strategy to Cope with Stress and Facilitates Development of Antibiotic Resistance.Scientific reports · 2020Article
- Tetracycline Antibiotics and Resistance.Cold Spring Harbor perspectives in medicine · 2016Review
- The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Clinical microbiology reviews · 2015Review
- Transcription Factors That Defend Bacteria Against Reactive Oxygen Species.Annual review of microbiology · 2015Review
- Complex structure of the DNA-binding domain of AdpA, the global transcription factor in Streptomyces griseus, and a target duplex DNA reveals the structural basis of its tolerant DNA sequence specificity.The Journal of biological chemistry · 2013Article
- Comparative genomics boosts target prediction for bacterial small RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- MarA, SoxS and Rob ofInternational journal of biotechnology for wellness industries · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Three paralogous transcriptional activators MarA, SoxS, and Rob, activate > 40 Escherichia coli promoters. To understand why MarA does not activate certain promoters as strongly as SoxS, we compared MarA, MarA mutants, and SoxS for their abilities to activate 16 promoters and to bind their cognate marbox binding sites. Replacement of the MarA glutamic acid residue 89 with alanine greatly increased the marbox binding and activation of many class I promoters. Like cells constitutive for SoxS, cells expressing the MarA with the E89A mutation were more resistant to superoxides than those harboring WT MarA. The activities of several other E89 substitutions ranked as follows: E89A > E89G > E89V > WT > E89D. Increased binding and activation occurred only at class I promoters when the 12th base of the promoter's marbox (a position at which there is no known interaction between the marbox and MarA) was not a T residue. Furthermore, WT MarA binding to a synthetic marbox in vitro was enhanced when the phosphate group between positions 12 and 13 was eliminated on one strand. The results demonstrate that relatively minor changes in a single amino acid side chain (e.g., alanine to valine or glutamic acid to aspartic acid) can strongly influence activity despite any evidence that the side chain is involved in positive interactions with either DNA or RNA polymerase. We present a model which attributes the differences in binding and activation to the interference between the β- and γ-carbons of the amino acid at position 89 and the phosphate group between positions 12 and 13.
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