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Related Experiment Videos

The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.

Michiko M Nakano1, Hao Geng, Shunji Nakano

  • 1Department of Environmental and Biomolecular Systems, OGI School of Science and Engineering, Oregon Health and Science University, 20000 NW Walker Road, Beaverton, OR 97006, USA. mnakano@ebs.ogi.edu

Journal of Bacteriology
|August 4, 2006
PubMed
Summary

NsrR regulates respiration in Bacillus subtilis by sensing nitric oxide (NO). Loss of NsrR disrupts NO-dependent gene expression, impacting aerobic and anaerobic respiration.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The ResD-ResE system controls aerobic and anaerobic respiration in Bacillus subtilis.
  • Oxygen limitation induces ResDE-dependent gene expression, with full induction under anaerobic conditions requiring nitrite or nitric oxide (NO).

Purpose of the Study:

  • To identify the regulator responsible for NO-dependent up-regulation of the ResDE regulon.
  • To elucidate the role of NsrR in regulating ResDE-controlled genes under varying oxygen and NO conditions.

Main Methods:

  • Gene expression analysis of hmp (flavohemoglobin gene) in wild-type and nsrR mutant Bacillus subtilis strains.
  • Investigating the effect of NO exposure on NsrR cellular concentration and activity.

Main Results:

Related Experiment Videos

  • NsrR mediates NO-dependent up-regulation of the ResDE regulon.
  • NsrR negatively regulates aerobic hmp expression and plays a crucial role in anaerobic regulation of ResDE targets.
  • B. subtilis lacking NsrR fails to sense and respond to NO for ResDE regulon up-regulation.
  • NO modulates NsrR activity, likely via its proposed Fe-S cluster, rather than changing its cellular concentration.

Conclusions:

  • NsrR is a key transcriptional repressor that integrates NO-sensing into the ResDE respiration regulatory network in Bacillus subtilis.
  • NsrR functions similarly to other bacterial NO-sensitive repressors, with NO interaction at its Fe-S center proposed to be the mechanism of activity modulation.