Role of rpoS (katF) in oxyR‐independent regulation of hydroperoxidase I in Escherichia coli

Ivanova, Anna; Miller, Carl F.; Glinsky, Gennadi V.; Eisenstark, A.

doi:10.1111/j.1365-2958.1994.tb01043.x

Cited by 109 publications

(83 citation statements)

References 23 publications

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“…This result supported the hypothesis that catalase I activity increased in response to elevated oxidative stress in the catalase II-deficient cells 18 . In summary, the data presented here suggests the existence of a secondary pathway for catalase I induction at the stationary phase of B. pseudomallei.…”

Section: Scienceasia Scienceasia Scienceasiasupporting

confidence: 87%

“…However, in this study we have cultured the bacteria in LB medium and found that at 72 and 96 h, the rpoS mutant strain showed a 31% and 29% survival rate (data not shown), indicating that cells in late stationary phase in rich media had a higher survival rate compared to those grown in minimal media. In E. coli, an increase of HPI catalase activity in stationary phase, attributed to RpoS-dependent transcription of katG has been reported 18 . In the rpoS mutants, these authors 15 detected little or no catalase activities by zymography assays.…”

Section: Discussionmentioning

confidence: 96%

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Jangiam¹,

Loprasert²,

Tungpradabkul³

2008

ScienceAsia

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Burkholderia pseudomallei is the causative agent of melioidosis. A previous study showed that the B. pseudomallei rpoS mutant is more sensitive to hydrogen peroxide than is the wild type strain, suggesting the RpoS may play a critical role in resistance to oxidative stress. Analysis of rpoS gene expression by β-galactosidase activity assay indicated that rpoS is activated when exposed to hydrogen peroxide on entry into the stationary phase. In addition, native gel electrophoresis and staining for catalase activities revealed that there are two types of catalases (I and II) in B. pseudomallei. Catalase I in the rpoS mutant exhibited higher activity than the parent strain, whereas catalase II was not detected in the rpoS mutant strain. Interestingly, even though catalase II was the prominent activity in the stationary phase culture of the wild type, it did not increase in response to hydrogen peroxide treatment. Construction of the B. pseudomallei katE mutant indicated that the katE gene encodes catalase II. Our experiments showed that katE is directly controlled by the RpoS and is not induced by hydrogen peroxide. These results suggest that the B. pseudomallei RpoS is activated under an oxidative stress condition and controls the activities of both catalases, I and II, in different manners.

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Section: Scienceasia Scienceasia Scienceasiasupporting

confidence: 87%

Section: Discussionmentioning

confidence: 96%

Untitled

Jangiam¹,

Loprasert²,

Tungpradabkul³

2008

ScienceAsia

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“…The two E. coli hydroperoxidases (catalases) were used as 'reporter genes' for RpoS-dependent transcription because both hydroperoxidase I (katG gene product, cytoplasmic membrane associated) and hydroperoxidase II (katE gene product, present in the cytosol) were shown to be regulated by s s (Ivanova et al, 1994), with hydroperoxidase II expression being entirely dependent on RpoS (Visick & Clarke, 1997). Hydroperoxidase I (HPI) and hydroperoxidase II (HPII) specific activities were measured as described by Visick & Clarke (1997).…”

Section: Methodsmentioning

confidence: 99%

Specific growth rate and not cell density controls the general stress response in Escherichia coli

2004

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In batch cultures of Escherichia coli, the intracellular concentration of the general stress response sigma factor RpoS typically increases during the transition from the exponential to the stationary growth phase. However, because this transition is accompanied by complex physico-chemical and biological changes, which signals predominantly elicit this induction is still the subject of debate. Careful design of the growth environment in chemostat and batch cultures allowed the separate study of individual factors affecting RpoS. Specific growth rate, and not cell density or the nature of the growth-limiting nutrient, controlled RpoS expression and RpoS-dependent hydroperoxidase activity. Furthermore, it was demonstrated that the standard E. coli minimal medium A (MMA) is not suitable for high-cell-density cultivation because it lacks trace elements. Previously reported cell-density effects in chemostat cultures of E. coli can be explained by a hidden, secondary nutrient limitation, which points to the importance of medium design and appropriate experimental set-up for studying cell-density effects.

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“…Although the basal expression of katG also depends on the RpoS level in stationary phase (30), the katG expression dependent on the OxyR activator may be sufficient to remove FIG. 2.…”

Section: Overproduction Of Polyphosphatase Decreases Poly(p) To Barelmentioning

confidence: 99%

Inorganic polyphosphate and the induction of rpoS expression

Shiba

Tsutsumi

Yano

et al. 1997

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

180

170

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Inorganic polyphosphate [poly(P)] levels in Escherichia coli were reduced to barely detectable concentrations by expression of the plasmid-borne gene for a potent yeast exopolyphosphatase [poly(P)ase]. As a consequence, resistance to H 2 O 2 was greatly diminished, particularly in katG (catalase HPI) mutants, implying a major role for the other catalase, the stationary-phase KatE (HPII), which is rpoS dependent. Resistance was restored to wild-type levels by complementation with plasmids expressing ppk, the gene for PPK [the polyphosphate kinase that generates poly(P)]. Induction of expression of both katE and rpoS (the stationaryphase factor) was prevented in cells in which the poly(P)ase was overproduced. Inasmuch as this inhibition by poly(P)ase did not affect the levels of the stringent-response guanosine nucleotides (pppGpp and ppGpp) and in view of the capacity of additional rpoS expression to suppress the poly(P)ase inhibition of katE expression, a role is proposed for poly(P) in inducing the expression of rpoS.

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Role of rpoS (katF) in oxyR‐independent regulation of hydroperoxidase I in Escherichia coli

Cited by 109 publications

References 23 publications

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Untitled

Specific growth rate and not cell density controls the general stress response in Escherichia coli

Inorganic polyphosphate and the induction of rpoS expression

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