Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in <i>Escherichia coli</i>

Ren, Binbin; Zhang, Nianhui; Yang, Juanjuan; Ding, Huangen

doi:10.1111/j.1365-2958.2008.06464.x

Cited by 66 publications

(90 citation statements)

References 38 publications

(106 reference statements)

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“…This enzyme is a stress-labile enzyme due to its Fe-S cluster (46,47). E. coli exposed to hyperbaric oxygen or nitric oxide becomes auxotrophic for branched-chain amino acids due to inactivation of IlvD (48)(49)(50). However, involvement of any ECF factors in ilvD expression has never been reported in bacteria to our knowledge.…”

Section: Resultsmentioning

confidence: 85%

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

et al. 2014

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bThe extracytoplasmic function sigma factor H is responsible for the heat and oxidative stress response in Corynebacterium glutamicum. Due to the hierarchical nature of the regulatory network, previous transcriptome analyses have not been able to discriminate between direct and indirect targets of H . Here, we determined the direct genome-wide targets of H using chromatin immunoprecipitation with microarray technology (ChIP-chip) for analysis of a deletion mutant of rshA, encoding an antifactor of H . Seventy-five H -dependent promoters, including 39 new ones, were identified. H -dependent, heat-inducible transcripts for several of the new targets, including ilvD encoding a labile Fe-S cluster enzyme, dihydroxy-acid dehydratase, were detected, and their 5= ends were mapped to the H -dependent promoters identified. Interestingly, functional internal H -dependent promoters were found in operon-like gene clusters involved in the pentose phosphate pathway, riboflavin biosynthesis, and Zn uptake. Accordingly, deletion of rshA resulted in hyperproduction of riboflavin and affected expression of Zn-responsive genes, possibly through intracellular Zn overload, indicating new physiological roles of H . Furthermore, sigA encoding the primary factor was identified as a new target of H . Reporter assays demonstrated that the H -dependent promoter upstream of sigA was highly heat inducible but much weaker than the known A -dependent one. Our ChIP-chip analysis also detected the H -dependent promoters upstream of rshA within the sigH-rshA operon and of sigB encoding a group 2 factor, supporting the previous findings of their H -dependent expression. Taken together, these results reveal an additional layer of the sigma factor regulatory network in C. glutamicum.

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Section: Resultsmentioning

confidence: 85%

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

et al. 2014

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“…NO improves gut motility 26 ; however, as described for priapism, 27 chronic NO depletion may change the sensitivity of smooth muscle to NO and disrupt normal protective feedback mechanisms, resulting in a robust response to a modest increase in NO because of infection/ inflammation. In addition, NO is bacteriostatic for several organisms, including Escherichia coli, 28 and bactericidal for some. 29 It may be that alteration in bowel flora by hydroxyurea somehow reduced the incidence of gastroenteritis.…”

Section: Discussionmentioning

confidence: 99%

Impact of hydroxyurea on clinical events in the BABY HUG trial

Thornburg

Files

Luo

et al. 2012

Blood

213

181

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The Pediatric Hydroxyurea Phase 3 Clinical Trial (BABY HUG) was a phase 3 multicenter, randomized, double-blind, placebocontrolled clinical trial of hydroxyurea in infants (beginning at 9-18 months of age) with sickle cell anemia. An important secondary objective of this study was to compare clinical events between the hydroxyurea and placebo groups. One hundred and ninetythree subjects were randomized to hy- Continuing Medical Education onlineThis activity has been planned and implemented in accordance with the Essential Areas and policies of the Accreditation Council for Continuing Medical Education through the joint sponsorship of Medscape, LLC and the American Society of Hematology. Medscape, LLC is accredited by the ACCME to provide continuing medical education for physicians. Medscape, LLC designates this Journal-based CME activity for a maximum of 1.0 AMA PRA Category 1 Credit(s) ™ . Physicians should claim only the credit commensurate with the extent of their participationin the activity. All other clinicians completing this activity will be issued a certificate of participation. To participate in this journal CME activity: (1) review the learning objectives and author disclosures; (2) study the education content; (3) take the post-test with a 70% minimum passing score and complete the evaluation at http://www.medscape.org/journal/blood; and (4) view/print certificate. For CME questions, see page 4448. Disclosures The authors, the Associate Editor Narla Mohandas, and CME questions author Laurie Barclay, freelance writer and reviewer, Medscape, LLC, declare no competing financial interests. Learning objectivesUpon completion of this activity, participants will be able to:1. Describe the effect of hydroxyurea on rates of sickle cell complications for infants with sickle cell anemia (SCA) on the basis of a phase 3, multicenter, randomized trial.2. Describe the effect of hydroxyurea on rates of hospitalizations and transfusions for infants with SCA on the basis of a phase 3, multicenter, randomized trial.3. Describe the safety of hydroxyurea for infants with SCA on the basis of a phase 3, multicenter, randomized trial.

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“…Most direct effects of NO on biological systems stem from its interaction with transition metals in terminal cytochromes of the electron transport chain and [4Fe-4S] prosthetic groups in dehydratases (5,6). The selectivity of NO for metalloproteins also applies to Salmonella, as shown by the nitrosylation of the bd quinol cytochrome oxidase (7); in that case, NO is a positive signal that stimulates the expression of antioxidant defenses.…”

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confidence: 99%

Redox sensor SsrB Cys ²⁰³ enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection

Husain¹,

Jones-Carson

Song³

et al. 2010

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

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We show herein that the Salmonella pathogenicity island 2 (SPI2) response regulator SsrB undergoes S-nitrosylation upon exposure of Salmonella to acidified nitrite, a signal encountered by this enteropathogen in phagosomes of macrophages. Mutational analysis has identified Cys 203 in the C-terminal dimerization domain of SsrB as the redox-active residue responding to nitric oxide (NO) congeners generated in the acidification of nitrite. Peroxynitrite and products of the autooxidation of NO in the presence of oxygen, but not hydrogen peroxide, inhibit the DNA-binding capacity of SsrB, demonstrating the selectivity of the reaction of Cys 203 with reactive nitrogen species (RNS). These findings identify the twocomponent response regulator SsrB Cys 203 as a thiol-based redox sensor. A C203S substitution protects SsrB against the attack of RNS while preserving its DNA-binding capacity. When exposed to SPI2-inducing conditions, Salmonella expressing the wild-type ssrB allele or the ssrB C203S variant sustain transcription of the sifA, sspH2, and srfJ effector genes. Nonetheless, compared with the strain expressing a redox-resistant SsrB C203S variant, wild-type Salmonella bearing the NO-responsive allele exhibit increased fitness when exposed to RNS in an NRAMP R , C3H/HeN murine model of acute oral infection. Given the widespread occurrence of the wildtype allele in Salmonella enterica, these findings indicate that SsrB Cys 203 increases Salmonella virulence by serving as a redox sensor of NO resulting from the host immune response to oral infection.macrophages | pathogenesis | two-component regulatory system

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Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in Escherichia coli

Cited by 66 publications

References 38 publications

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

Impact of hydroxyurea on clinical events in the BABY HUG trial

Redox sensor SsrB Cys ²⁰³ enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection

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Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in Escherichia coli

Cited by 66 publications

References 38 publications

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σHin Corynebacterium glutamicum

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σHin Corynebacterium glutamicum

Impact of hydroxyurea on clinical events in the BABY HUG trial

Redox sensor SsrB Cys 203 enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection

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Product

Resources

About

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

Expanding the Regulatory Network Governed by the Extracytoplasmic Function Sigma Factor σ^Hin Corynebacterium glutamicum

Redox sensor SsrB Cys ²⁰³ enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection