A Role for Sigma Factor σE in Corynebacterium pseudotuberculosis Resistance to Nitric Oxide/Peroxide Stress

ABSTRACT The rpoN region of Pseudomonas stutzeri was cloned, and an rpoN null mutant was constructed. RpoN was not essential for denitrification in this bacterium but affected the expression levels and enzymatic activities of cytochromecd 1 nitrite reductase and nitric oxide reductase, whereas those of respiratory nitrate reductase and nitrous oxide reductase were comparable to wild-type levels. Since the transcription of the structural genes nirS andnorCB, coding for nitrite reductase and the nitric oxide reductase complex, respectively, proceeded unabated, our data indicate a posttranslational process for the two key enzymes of denitrification depending on RpoN.

Download Full-text

Label-free proteomic analysis to confirm the predicted proteome of Corynebacterium pseudotuberculosis under nitrosative stress mediated by nitric oxide

BMC Genomics ◽

10.1186/1471-2164-15-1065 ◽

2014 ◽

Vol 15 (1) ◽

pp. 1065 ◽

Cited By ~ 12

Author(s):

Wanderson M Silva ◽

Rodrigo D Carvalho ◽

Siomar C Soares ◽

Isabela FS Bastos ◽

Edson L Folador ◽

...

Keyword(s):

Nitric Oxide ◽

Proteomic Analysis ◽

Nitrosative Stress ◽

Corynebacterium Pseudotuberculosis ◽

Label Free

Download Full-text

Involvement of the Mannose Phosphotransferase System of Lactobacillus plantarum WCFS1 in Peroxide Stress Tolerance

Applied and Environmental Microbiology ◽

10.1128/aem.00073-10 ◽

2010 ◽

Vol 76 (11) ◽

pp. 3748-3752 ◽

Cited By ~ 21

Author(s):

Marc J. A. Stevens ◽

Douwe Molenaar ◽

Anne de Jong ◽

Willem M. de Vos ◽

Michiel Kleerebezem

Keyword(s):

Stress Response ◽

Stress Tolerance ◽

Lactobacillus Plantarum ◽

Sigma Factor ◽

Parental Strain ◽

Alternative Sigma Factor ◽

Wild Type ◽

Phosphotransferase System ◽

Higher Sensitivity ◽

Peroxide Stress

ABSTRACT A Lactobacillus plantarum strain with a deletion in the gene rpoN, encoding the alternative sigma factor 54 (σ54), displayed a 100-fold-higher sensitivity to peroxide than its parental strain. This feature could be due to σ54-dependent regulation of genes involved in the peroxide stress response. However, transcriptome analyses of the wild type and the mutant strain during peroxide exposure did not support such a role for σ54. Subsequent experiments revealed that the impaired expression of the mannose phosphotransferase system (PTS) operon in the rpoN mutant caused the observed increased peroxide sensitivity.

Download Full-text

Localization of endothelial nitric oxide synthase in the normal and failing human atrial myocardium

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100166397 ◽

1996 ◽

Vol 54 ◽

pp. 786-787

Author(s):

Chi-Ming Wei ◽

Margarita Bracamonte ◽

Shi-Wen Jiang ◽

Richard C. Daly ◽

Christopher G.A. McGregor ◽

...

Keyword(s):

Nitric Oxide ◽

Heart Failure ◽

Nitric Oxide Synthase ◽

Endothelial Nitric Oxide Synthase ◽

Cardiac Tissues ◽

Mammalian Tissues ◽

End Stage Heart Failure ◽

End Stage ◽

Oxide Synthase ◽

Endothelial Nitric Oxide

Nitric oxide (NO) is a potent endothelium-derived relaxing factor which also may modulate cardiomyocyte inotropism and growth via increasing cGMP. While endothelial nitric oxide synthase (eNOS) isoforms have been detected in non-human mammalian tissues, expression and localization of eNOS in the normal and failing human myocardium are poorly defined. Therefore, the present study was designed to investigate eNOS in human cardiac tissues in the presence and absence of congestive heart failure (CHF).Normal and failing atrial tissue were obtained from six cardiac donors and six end-stage heart failure patients undergoing primary cardiac transplantation. ENOS protein expression and localization was investigated utilizing Western blot analysis and immunohistochemical staining with the polyclonal rabbit antibody to eNOS (Transduction Laboratories, Lexington, Kentucky).

Download Full-text