Structural Analysis of the DNA-binding Domain of the Helicobacter pylori Response Regulator ArsR

Gupta, Shobhana Satyendra; Borin, Brendan N.; Cover, Timothy L.; Krezel, Andrzej M.

doi:10.1074/jbc.m804592200

Cited by 19 publications

(22 citation statements)

References 51 publications

(81 reference statements)

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“…In turn, the phosphate group is transferred to the response regulator ArsR, a protein belonging to the OmpR family. The DNA‐binding domain of the latter is quite similar to that of the other members of the OmpR/PhoB subfamily of bacterial response regulators, consisting of an N‐terminal four‐stranded β‐sheet, a helical core, and a C‐terminal β‐hairpin (32). It contains winged helix‐turn‐helix (HTH) motif that is predicted to bind DNA.…”

Section: Introductionmentioning

confidence: 99%

Functional and structural aspects of helicobacter pylori acidic stress response factors

Zanotti

Cendron

2010

IUBMB Life

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SummaryHelicobacter pylori is a striking example of adaptation of a bacterium to a very peculiar niche, the human stomach. Despite being a neutralophile, a sophisticated control of gene expression allows it to live and to proliferate in an environment that cycles from nearly neutral to very acidic. Despite the numerous studies performed on the mechanisms of acid adaptation, the physiological function of a large part of the genes products that are up-regulated or down-regulated is often not clear, in particular in the context of the response of the bacterium to an acidic stress. In this review, we discuss the molecular and functional aspects of some of the proteins that are commonly found overexpressed during the acid stress.

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Section: Introductionmentioning

confidence: 99%

Functional and structural aspects of helicobacter pylori acidic stress response factors

Zanotti

Cendron

2010

IUBMB Life

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“…Full-length (26-kDa) ArsR and the DNA-binding domain of ArsR (13 kDa) were expressed in E. coli and purified as described previously (20). The primers listed in Table S1 in the supplemental material were used to PCR amplify 100-to 150-bp regions located upstream of the translation initiation sites of the selected target genes.…”

Section: Methodsmentioning

confidence: 99%

“…The ArsRS two-component signal transduction system has an important role in allowing H. pylori to sense and regulate target genes in response to changes in pH and is required for colonization of the stomach (25, 29, 31-33, 50, 51). This twocomponent system is comprised of a sensor kinase (ArsS, corresponding to HP0165 in H. pylori 26695) and a response regulator (ArsR, corresponding to HP0166) (20,28; reviewed in references 21 and 34). The ArsRS two-component system regulates multiple genes involved in acid resistance, including genes encoding members of the urease complex (33), amidases (32), and carbonic anhydrase (50).…”

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confidence: 99%

Analysis of Protein Expression Regulated by theHelicobacter pyloriArsRS Two-Component Signal Transduction System

Loh¹,

Gupta

Friedman

et al. 2010

J Bacteriol

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Previous studies have shown that the Helicobacter pylori ArsRS two-component signal transduction system contributes to acid-responsive gene expression. To identify additional members of the ArsRS regulon and further investigate the regulatory role of the ArsRS system, we analyzed protein expression in wild-type and arsS null mutant strains. Numerous proteins were differentially expressed in an arsS mutant strain compared to a wild-type strain when the bacteria were cultured at pH 5.0 and also when they were cultured at pH 7.0. Genes encoding 14 of these proteins were directly regulated by the ArsRS system, based on observed binding of ArsR to the relevant promoter regions. The ArsRS-regulated proteins identified in this study contribute to acid resistance (urease and amidase), acetone metabolism (acetone carboxylase), resistance to oxidative stress (thioredoxin reductase), quorum sensing (Pfs), and several other functions. These results provide further definition of the ArsRS regulon and underscore the importance of the ArsRS system in regulating expression of H. pylori proteins during bacterial growth at both neutral pH and acidic pH.

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“…HP1264 folds into a compact two-layered α/β-sandwich structure with the topology described as β-α-β-α-β-β, comprising a mixed four-stranded β-sheet stacked against two α-helices, both of which are nearly parallel to the strands of the β-sheet. The β-strands correspond to the residues 3-5 (βI), 28-35 (βII), 55-57 (βIII), and 68-74 (βIV), while the α-helices correspond to the residues 20-24 (αI) and [40][41][42][43][44][45][46][47][48][49][50]. Based on the SCOP database, it is revealed that HP1264 adopts an IF3 (translation initiation factor 3)-like fold.…”

Section: Proteins Between 20 and 99 Amino Acid Residues: 1yg0 1zhc mentioning

confidence: 99%

“…2K4J, H. pylori ArsS-ArsR two-component signal transduction system, comprised of a sensor histidine kinase (ArsS) and a response regulator (ArsR), allows the bacteria to regulate gene expression in response to acidic pH conditions [47]. Full-length ArsR protein and the DNA-binding domain of ArsR (ArsR-DBD) were expressed and purified, and the structure of the ArsR-DBD was solved.…”

Section: Proteins Between 100 and 200 Amino Acid Residues: 2hqn 1x93mentioning

confidence: 99%

NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review

2013

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Due to the widespread and increasing appearance of antibiotic resistance, a new strategy is needed for developing novel antibiotics. Especially, there are no specific antibiotics for Helicobacter pylori (H. pylori). H. pylori are bacteria that live in the stomach and are related to many serious gastric problems such as peptic ulcers, chronic gastritis, mucosa-associated lymphoid tissue lymphoma, and gastric cancer. Because of its importance as a human pathogen, it's worth studying the structure and function of the proteins from H. pylori. After the sequencing of the H. pylori strain 26695 in 1997, more than 1,600 genes were identified from H. pylori. Until now, the structures of 334 proteins from H. pylori have been determined. Among them, 309 structures were determined by X-ray crystallography and 25 structures by Nuclear Magnetic Resonance (NMR), respectively. Overall, the structures of large proteins were determined by X-ray crystallography and those of small proteins by NMR. In our lab, we have studied the structural and functional characteristics of small proteins from H. pylori. In this review, 25 NMR structures of H. pylori proteins will be introduced and their structure-function relationships will be discussed.

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Structural Analysis of the DNA-binding Domain of the Helicobacter pylori Response Regulator ArsR

Cited by 19 publications

References 51 publications

Functional and structural aspects of helicobacter pylori acidic stress response factors

Functional and structural aspects of helicobacter pylori acidic stress response factors

Analysis of Protein Expression Regulated by theHelicobacter pyloriArsRS Two-Component Signal Transduction System

NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review

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