Literature DB >> 12855179

Vitreoscilla hemoglobin promoter is not responsive to nitrosative and oxidative stress in Escherichia coli.

Alexander D Frey1, Taija Koskenkorva, Pauli T Kallio.   

Abstract

The Vitreoscilla hemoglobin gene (vhb) is expressed under oxygen-limited conditions via an FNR-dependent mechanism. Furthermore, cAMP-CRP has been implicated in its regulation. Recently, VHb protein has been reported to protect a heterologous host from nitrosative stress. In this study we analyzed the regulation of the Vitreoscilla hemoglobin promoter (Pvhb) in Escherichia coli under nitrosative and oxidative stress conditions. Our results show unambiguously that expression of neither VHb nor chloramphenicol acetyltransferase under the control of Pvhb is induced under the experimental conditions used. Thus, a clear discrepancy between in vivo function, i.e. protection against nitrosative stress, and regulation of gene expression is obvious. The regulation of Pvhb reported here is in clear contrast to the expression pattern of flavohemoglobins from various microorganisms, which are generally induced by nitrosative stress. However, the length of Pvhb is only 146 bp and therefore, we cannot rule out that additional regulatory sequences may be located in the upstream region of Pvhb.

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Year:  2003        PMID: 12855179     DOI: 10.1016/S0378-1097(03)00434-8

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  2 in total

Review 1.  Hemoglobin: a nitric-oxide dioxygenase.

Authors:  Paul R Gardner
Journal:  Scientifica (Cairo)       Date:  2012-12-19

2.  Role of an inducible single-domain hemoglobin in mediating resistance to nitric oxide and nitrosative stress in Campylobacter jejuni and Campylobacter coli.

Authors:  Karen T Elvers; Guanghui Wu; Nicola J Gilberthorpe; Robert K Poole; Simon F Park
Journal:  J Bacteriol       Date:  2004-08       Impact factor: 3.490

  2 in total

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