Identification of
            <i>Bacillus subtilis</i>
            CysL, a Regulator of the
            <i>cysJI</i>
            Operon, Which Encodes Sulfite Reductase

Guillouard, Isabelle; Auger, Sandrine; Hullo, Marie-Françoise; Chetouani, Farid; Danchin, Antoine; Martin‐Verstraete, Isabelle

doi:10.1128/jb.184.17.4681-4689.2002

Cited by 48 publications

(44 citation statements)

References 38 publications

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“…However, the sulfate assimilation pathway is regulated by CysB but not by CymR under the conditions tested (Table 2). In B. subtilis, the expression of the cysJI operon, encoding the sulfite reductase, is positively regulated by the CysL activator (11). These two organisms have retained different strategies of regulation: an LysR-type activator, CysB, in E. coli and an Rrf2-type repressor, CymR, in B. subtilis.…”

Section: Discussionmentioning

confidence: 99%

“…Primers IV152 (5Ј-CCTGCTAAAAATACCCCTAATTT-3Ј) and SA54 (5Ј-AAGAGCCCTAAGATAAGTAAAAATAAA-3Ј) were used for primer extension on yxeK and tcyP, respectively. Primer extension experiments were performed as previously described (11).…”

Section: Vol 188 2006 Regulation Of Cysteine Metabolism 2185mentioning

confidence: 99%

“…In addition, two LysR-type regulators, CysL and YtlI, play a role in the regulation of sulfur metabolism. CysL positively controls expression of the cysJI operon encoding the sulfite reductase by binding to its promoter region (11). YtlI is a positive regulator of the ytmI operon, as discussed above (6).…”

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confidence: 99%

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Global Control of Cysteine Metabolism by CymR inBacillus subtilis

et al. 2006

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YrzC has previously been identified as a repressor controlling ytmI expression via its regulation of YtlI activator synthesis in Bacillus subtilis. We identified YrzC as a master regulator of sulfur metabolism. Gene expression profiles of B. subtilis ⌬yrzC mutant and wild-type strains grown in minimal medium with sulfate as the sole sulfur source were compared. In the mutant, increased expression was observed for 24 genes previously identified as repressed in the presence of sulfate. Since several genes involved in the pathways leading to cysteine formation were found, we propose to rename YrzC CymR, for "cysteine metabolism repressor." A CymR-dependent binding to the promoter region of the ytlI, ssuB, tcyP, yrrT, yxeK, cysK, or ydbM gene was demonstrated using gel shift experiments. A potential CymR target site, TAAWNCN 2 ANTWNAN 3 ATMGGAA TTW, was found in the promoter region of these genes. In a DNase footprint experiment, the protected region in the ytlI promoter region contained this consensus sequence. Partial deletion or introduction of point mutations in this sequence confirmed its involvement in ytlI, yrrT, and yxeK regulation. The addition of O-acetylserine in gel shift experiments prevented CymR-dependent binding to DNA for all of the targets characterized. Transcriptome analysis of a ⌬cymR mutant and the wild-type strain also brought out significant changes in the expression level of a large set of genes related to stress response or to transition toward anaerobiosis.

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Section: Discussionmentioning

confidence: 99%

Section: Vol 188 2006 Regulation Of Cysteine Metabolism 2185mentioning

confidence: 99%

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Global Control of Cysteine Metabolism by CymR inBacillus subtilis

et al. 2006

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“…As for regulation of transcription initiation, LysR-type regulators show operon-specific activity. For example, CysL and YtlI activate transcription of cysIJ (sulfite reductase) and ytmI (sulfonate utilization and cysteine transport), respectively (8,11,19).…”

Section: Discussionmentioning

confidence: 99%

The Global Regulator Spx Functions in the Control of Organosulfur Metabolism inBacillus subtilis

et al. 2006

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Spx is a global transcriptional regulator of the oxidative stress response in Bacillus subtilis. Its target is RNA polymerase, where it contacts the ␣ subunit C-terminal domain. Recently, evidence was presented that Spx participates in sulfate-dependent control of organosulfur utilization operons, including the ytmI, yxeI, ssu, and yrrT operons. The yrrT operon includes the genes that function in cysteine synthesis from S-adenosylmethionine through intermediates S-adenosylhomocysteine, ribosylhomocysteine, homocysteine, and cystathionine. These operons are also negatively controlled by CymR, the repressor of cysteine biosynthesis operons. All of the operons are repressed in media containing cysteine or sulfate but are derepressed in medium containing the alternative sulfur source, methionine. Spx was found to negatively control the expression of these operons in sulfate medium, in part, by stimulating the expression of the cymR gene. In addition, microarray analysis, monitoring of yrrT-lacZ fusion expression, and in vitro transcription studies indicate that Spx directly activates yrrT operon expression during growth in medium containing methionine as sole sulfur source. These experiments have uncovered additional roles for Spx in the control of gene expression during unperturbed, steadystate growth.The global regulator Spx of Bacillus subtilis functions in the oxidative stress response by activating transcription of genes that function in thiol homeostasis (33,34,49). In this capacity, it is required for the transcriptional activation of the thioredoxin (trxA) and thioredoxin reductase (trxB) genes in response to disulfide stress. It also represses genes that function in a variety of metabolic and developmental pathways (34,35). The activity and synthesis of Spx are stimulated when cells undergo accelerated disulfide generation resulting from encounters with toxic oxidants. The accumulated Spx interacts with RNA polymerase (RNAP) in part by contacting residues of the alpha subunit C-terminal domain (CTD), while showing no sequence-specific DNA-binding activity (36). An important feature of Spx is the N-terminal CxxC redox disulfide motif that controls Spx activity. Transcriptional activation from the trxA and trxB promoters requires that the two cysteines be in the oxidized, disulfide state. The presence of a reductant that converts the cysteines to the thiol state results in loss of transcription-stimulating activity (33). It is currently not known how the interaction of oxidized Spx protein with RNA polymerase activates transcription at promoters under Spx positive control.In addition to its role in oxidative stress, recent studies indicate that Spx functions as a regulator of gene expression in cells undergoing steady-state growth. Spx was found to negatively affect the transcription of genes that function in the utilization of organosulfur compounds as alternative sources of sulfur (13). Such operons are repressed in minimal glucose media containing either of the two preferred sulfur sources, sulfate and cys...

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“…Total RNA extraction from B. anthracis RTC50 was adapted from the protocol described by Guillouard et al for B. subtilis and using the Trizol reagent (Invitrogen) (15). The quality of RNA preparations was analyzed on an RNA NanoLabChip (Agilent Technologies).…”

Section: Methodsmentioning

confidence: 99%

CapE, a 47-Amino-Acid Peptide, Is Necessary for Bacillus anthracis Polyglutamate Capsule Synthesis

2005

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Polyglutamate is found in various bacteria, but displays different functions depending on the species and their environment. Here, we describe a minimal polyglutamate synthesis system in Bacillus anthracis. In addition to the three genes previously described as sufficient for polyglutamate synthesis, this system includes a small open reading frame, capE, belonging to the cap operon. The polyglutamate system's requirement for the five cap genes, for capsulation and anchoring, was assayed in nonpolar mutants. The capA, capB, capC, and capE genes are all necessary and are sufficient for polyglutamate synthesis by B. anthracis. capD is required for polyglutamate anchoring to the peptidoglycan. The 47-amino-acid peptide encoded by capE is localized in the B. anthracis membrane. It is not a regulator and it is required for polyglutamate synthesis, suggesting that it has a structural role in polyglutamate synthesis. CapE appears to interact with CapA. Bacillus subtilis ywtC is similar to capE and we named it pgsE. Genes similar to capE or pgsE were found in B. subtilis natto, Bacillus licheniformis, and Staphylococcus epidermidis, species that produce polyglutamate. All the bacterial polyglutamate synthesis systems analyzed show a similar genetic organization and, we suggest, the same protein requirements.

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Identification of Bacillus subtilis CysL, a Regulator of the cysJI Operon, Which Encodes Sulfite Reductase

Cited by 48 publications

References 38 publications

Global Control of Cysteine Metabolism by CymR inBacillus subtilis

Global Control of Cysteine Metabolism by CymR inBacillus subtilis

The Global Regulator Spx Functions in the Control of Organosulfur Metabolism inBacillus subtilis

CapE, a 47-Amino-Acid Peptide, Is Necessary for Bacillus anthracis Polyglutamate Capsule Synthesis

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