PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox

Zhulin, Igor B.; Taylor, Barry; Dixon, Ray

doi:10.1016/s0968-0004(97)01110-9

Cited by 392 publications

(327 citation statements)

References 12 publications

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“…In the 13 TCSTSs in S. mutans, only the VicK protein harbors a PAS domain, and PAS domains are almost exclusively sensors of oxygen and intracellular redox potential (37). In E. coli the aerotaxis transducer Aer has a PAS domain in its N-terminal region that promotes cell migration to a microenvironment with a preferred redox potential (26,27,36,41). As S. mutans is a member of the human oral microbial consortium that is usually exposed to various oxidative stresses, the ability of this organism to monitor intracellular oxygen levels is important because reactive oxygen radicals can be highly toxic to the cell.…”

Section: Discussionmentioning

confidence: 99%

The Streptococcus mutans vicX Gene Product Modulates gtfB / C Expression, Biofilm Formation, Genetic Competence, and Oxidative Stress Tolerance

et al. 2007

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Streptococcus mutans is considered one of the primary etiologic agents of dental caries. Previously, we characterized the VicRK two-component signal transduction system, which regulates multiple virulence factors of S. mutans. In this study, we focused on the vicX gene of the vicRKX tricistronic operon. To characterize vicX, we constructed a nonpolar deletion mutation in the vicX coding region in S. mutans UA159. The growth kinetics of the mutant (designated SmuvicX) showed that the doubling time was longer and that there was considerable sensitivity to paraquat-induced oxidative stress. Supplementing a culture of the wild-type UA159 strain with paraquat significantly increased the expression of vicX (P < 0.05, as determined by analysis of variance [ANOVA]), confirming the role of this gene in oxidative stress tolerance in S. mutans. Examination of mutant biofilms revealed architecturally altered cell clusters that were seemingly denser than the wild-type cell clusters. Interestingly, vicX-deficient cells grown in a glucose-supplemented medium exhibited significantly increased glucosyltransferase B/C (gtfB/C) expression compared with the expression in the wild type (P < 0.05, as determined by ANOVA). Moreover, a sucrose-dependent adhesion assay performed using an S. mutans GS5-derived vicX null mutant demonstrated that the adhesiveness of this mutant was enhanced compared with that of the parent strain and isogenic mutants of the parent strain lacking gtfB and/or gtfC. Also, disruption of vicX reduced the genetic transformability of the mutant approximately 10-fold compared with that of the parent strain (P < 0.05, as determined by ANOVA). Collectively, these findings provide insight into important phenotypes controlled by the vicX gene product that can impact S. mutans pathogenicity.

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Section: Discussionmentioning

confidence: 99%

The Streptococcus mutans vicX Gene Product Modulates gtfB / C Expression, Biofilm Formation, Genetic Competence, and Oxidative Stress Tolerance

et al. 2007

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“…The NifL protein resembles histidine kinase protein (HPK), but NifL is not subject to autophosphorylation. The amino-terminal region contains a PAS domain, and it has been proposed that this region may be involved in O 2 sensing (Zhulin et al, 1997). The C-terminal region shows similarity to the GHKL superfamily of ATPases.…”

Section: Introductionmentioning

confidence: 99%

Interaction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501

et al. 2006

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Pseudomonas stutzeri strain A1501 isolated from rice fixes nitrogen under microaerobic conditions in the free-living state. This paper describes the properties of nifL and nifA mutants as well as the physical interaction between NifL and NifA proteins. A nifL mutant strain that carried a mutation nonpolar on nifA expression retained nitrogenase activity. Complementation with a plasmid containing only nifL led to a decrease in nitrogenase activity in both the wild-type and the nifL mutant, suggesting that NifL acts as an antiactivator of NifA activity. Using the yeast two-hybrid system and purified protein domains of NifA and NifL, an interaction was shown between the C-terminal domain of NifL and the central domain of NifA, suggesting that NifL antiactivator activity is mediated by direct protein interaction with NifA.

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“…[15][16][17][18]. In addition to their sensory functions, PAS domains have been reported to mediate protein-protein interactions (18).…”

mentioning

confidence: 99%

Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction

Crosson

Moffat

2001

Proc. Natl. Acad. Sci. U.S.A.

465

539

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PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox

Cited by 392 publications

References 12 publications

The Streptococcus mutans vicX Gene Product Modulates gtfB / C Expression, Biofilm Formation, Genetic Competence, and Oxidative Stress Tolerance

The Streptococcus mutans vicX Gene Product Modulates gtfB / C Expression, Biofilm Formation, Genetic Competence, and Oxidative Stress Tolerance

Interaction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501

Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction

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