ArticleMicrobiology (Reading, England)2010
Functional roles for the GerE-family carboxyl-terminal domains of nitrate response regulators NarL and NarP of Escherichia coli K-12.
Article in Microbiology (Reading, England), 2010. 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.
- Structural basis for transcription activation by the nitrate-responsive regulator NarL.Nucleic acids research · 2024Article
- Structural and biochemical analyses of the flagellar expression regulator DegU from Listeria monocytogenes.Scientific reports · 2022Article
- Activation by NarL at the Escherichia coli ogt promoter.The Biochemical journal · 2020Article
- Pneumococcal vaccine impacts on the population genomics of non-typeable Haemophilus influenzae.Microbial genomics · 2018Article
- Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution.Journal of bacteriology · 2015Article
- The Escherichia coli NarL receiver domain regulates transcription through promoter specific functions.BMC microbiology · 2015Article
- Sensor-response regulator interactions in a cross-regulated signal transduction network.Microbiology (Reading, England) · 2015Article
- Essentiality of DevR/DosR interaction with SigA for the dormancy survival program in Mycobacterium tuberculosis.Journal of bacteriology · 2014Article
- Transcriptional regulation of the ecp operon by EcpR, IHF, and H-NS in attaching and effacing Escherichia coli.Journal of bacteriology · 2012Article
- Output targets and transcriptional regulation by a cyclic dimeric GMP-responsive circuit in the Vibrio parahaemolyticus Scr network.Journal of bacteriology · 2012Article
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2 authors.
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Abstract
NarL and NarP are paralogous response regulators that control anaerobic gene expression in response to the favoured electron acceptors nitrate and nitrite. Their DNA-binding carboxyl termini are in the widespread GerE-LuxR-FixJ subfamily of tetrahelical helix-turn-helix domains. Previous biochemical and crystallographic studies with NarL suggest that dimerization and DNA binding by the carboxyl-terminal domain (CTD) is inhibited by the unphosphorylated amino-terminal receiver domain. We report here that NarL-CTD and NarP-CTD, liberated from their receiver domains, activated transcription in vivo from the class II napF and yeaR operon control regions, but failed to activate from the class I narG and fdnG operon control regions. Alanine substitutions were made to examine requirements for residues in the NarL DNA recognition helix. Substitutions for Val-189 and Arg-192 blocked DNA binding as assayed both in vivo and in vitro, whereas substitution for Arg-188 had a strong effect only in vivo. Similar results were obtained with the corresponding residues in NarP. Finally, Ala substitutions identified residues within the NarL CTD as important for transcription activation. Overall, results are congruent with those obtained for other GerE-family members, including GerE, TraR, LuxR and FixJ.
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