In vivo studies of the activity of four of the kinases, KinA, [PROTEIN1] KinC [/PROTEIN1], KinD (ykvD) and KinE (ykrQ), using abrB transcription as an indicator of [PROTEIN2] Spo0A~P [/PROTEIN2] level, revealed that KinC and KinD were responsible for Spo0A~P production during the exponential phase of growth in the absence of KinA and KinB.


In vivo studies of the activity of four of the kinases, KinA, KinC, [PROTEIN1] KinD [/PROTEIN1] (ykvD) and KinE (ykrQ), using abrB transcription as an indicator of [PROTEIN2] Spo0A~P [/PROTEIN2] level, revealed that KinC and KinD were responsible for Spo0A~P production during the exponential phase of growth in the absence of KinA and KinB.


In this mutant, expression of the [PROTEIN2] spoIIG [/PROTEIN2] gene, whose transcription depends on both [PROTEIN1] sigma(A) [/PROTEIN1] and the phosphorylated Spo0A protein, Spo0A~P, a major transcription factor during early stages of sporulation, was greatly reduced at 43 degrees C.


In this mutant, expression of the [PROTEIN2] spoIIG [/PROTEIN2] gene, whose transcription depends on both sigma(A) and the phosphorylated [PROTEIN1] Spo0A [/PROTEIN1] protein, Spo0A~P, a major transcription factor during early stages of sporulation, was greatly reduced at 43 degrees C.


Transcription of [PROTEIN2] ydhD [/PROTEIN2] was dependent on [PROTEIN1] SigE [/PROTEIN1], and the mRNA was detectable from 2 h after the cessation of logarithmic growth (T2 of sporulation).


[PROTEIN2] ykuD [/PROTEIN2] was transcribed by [PROTEIN1] SigK [/PROTEIN1] RNA polymerase from T4 of sporulation.


Both [PROTEIN1] SigK [/PROTEIN1] and GerE were essential for [PROTEIN2] ykvP [/PROTEIN2] expression, and this gene was transcribed from T5 of sporulation.


Both SigK and [PROTEIN1] GerE [/PROTEIN1] were essential for [PROTEIN2] ykvP [/PROTEIN2] expression, and this gene was transcribed from T5 of sporulation.


Analysis of the expression of a translational [PROTEIN1] ywhE [/PROTEIN1]-lacZ fusion showed that ywhE expression is sporulation-specific, and is controlled predominantly by the forespore-specific sigma factor [PROTEIN1] sigma(F) [/PROTEIN1], and to a lesser extent by sigma(G).


Secondly, [PROTEIN1] SpoIIE [/PROTEIN1] is essential for the activation of the first compartment-specific transcription factor [PROTEIN2] sigma(F) [/PROTEIN2] in the prespore.


Localization of [PROTEIN2] SpoIIE [/PROTEIN2] was shown to be dependent on the essential cell division protein [PROTEIN1] FtsZ [/PROTEIN1].


In the shaA mutant, [PROTEIN1] sigma(H) [/PROTEIN1]-dependent expression of spo0A and [PROTEIN2] spoVG [/PROTEIN2] at an early stage of sporulation was sensitive to external NaCl.


The expression of [PROTEIN2] rsfA [/PROTEIN2] is under the control of both [PROTEIN1] sigma(F) [/PROTEIN1] and sigma(G).


Expression of the sigma(K)-dependent [PROTEIN2] cwlH [/PROTEIN2] gene depended on [PROTEIN1] gerE [/PROTEIN1].


promoter-based regulation of transcription

The -10 and -35 sequences of the [PROTEIN1] sigmaB [/PROTEIN1]- and sigmaF-dependent promoters of [PROTEIN2] katX [/PROTEIN2] overlap, and the transcriptional start points used by EsigmaB and EsigmaF differ by only one nucleotide.


The -10 and -35 sequences of the sigmaB- and [PROTEIN1] sigmaF [/PROTEIN1]-dependent promoters of [PROTEIN2] katX [/PROTEIN2] overlap, and the transcriptional start points used by EsigmaB and EsigmaF differ by only one nucleotide.


We demonstrated that [PROTEIN2] katX [/PROTEIN2] is also a [PROTEIN1] sigmaB [/PROTEIN1]-dependent general stress gene, since it is strongly induced by heat, salt and ethanol stress, as well as by energy depletion.


Taken together, the results support the idea that sequestration of [PROTEIN1] SpoIIE [/PROTEIN1] protein into the prespore plays an important role in the control of [PROTEIN2] sigmaF [/PROTEIN2] activation and in coupling this activation to septation.


[PROTEIN2] sigmaF [/PROTEIN2] is controlled by a regulatory cascade involving an anti-sigma factor, SpoIIAB, an anti-anti-sigma factor, [PROTEIN1] SpoIIAA [/PROTEIN1], and a membrane-bound phosphatase, SpoIIE, which converts the inactive, phosphorylated form of SpoIIAA back to the active form.


[PROTEIN2] sigmaF [/PROTEIN2] is controlled by a regulatory cascade involving an anti-sigma factor, SpoIIAB, an anti-anti-sigma factor, SpoIIAA, and a membrane-bound phosphatase, [PROTEIN1] SpoIIE [/PROTEIN1], which converts the inactive, phosphorylated form of SpoIIAA back to the active form.


sigmaF is controlled by a regulatory cascade involving an anti-sigma factor, SpoIIAB, an anti-anti-sigma factor, [PROTEIN2] SpoIIAA [/PROTEIN2], and a membrane-bound phosphatase, [PROTEIN1] SpoIIE [/PROTEIN1], which converts the inactive, phosphorylated form of SpoIIAA back to the active form.


The [PROTEIN2] rocG [/PROTEIN2] gene of Bacillus subtilis, encoding a catabolic glutamate dehydrogenase, is transcribed by [PROTEIN1] SigL [/PROTEIN1]-containing RNA polymerase and requires for its expression RocR, a member of the NtrC/NifA family of proteins that bind to enhancer-like elements, called upstream activating sequences (UAS).


Northern blot and primer extension analyses indicated that [PROTEIN2] yfhS [/PROTEIN2] is transcribed by [PROTEIN1] E sigma E [/PROTEIN1] during sporulation.


nmod:for(regulator, transcription); amod(regulator, negative)

These results suggest that [PROTEIN1] YfhP [/PROTEIN1] may act as a negative regulator for the transcription of [PROTEIN2] yfhQ [/PROTEIN2], yfhR, sspE and yfhP.


These results suggest that [PROTEIN1] YfhP [/PROTEIN1] may act as a negative regulator for the transcription of yfhQ, [PROTEIN2] yfhR [/PROTEIN2], sspE and yfhP.


These results suggest that [PROTEIN1] YfhP [/PROTEIN1] may act as a negative regulator for the transcription of yfhQ, yfhR, [PROTEIN2] sspE [/PROTEIN2] and yfhP.


These results suggest that [PROTEIN1] YfhP [/PROTEIN1] may act as a negative regulator for the transcription of yfhQ, yfhR, sspE and [PROTEIN2] yfhP [/PROTEIN2].


Production of [PROTEIN1] sigmaK [/PROTEIN1] about 1 h earlier than normal does affect [PROTEIN2] Spo0A [/PROTEIN2], which when phosphorylated is an activator of sigE transcription.


activation of gene transcription by phosphorylated protein

Production of sigmaK about 1 h earlier than normal does affect [PROTEIN1] Spo0A [/PROTEIN1], which when phosphorylated is an activator of [PROTEIN2] sigE [/PROTEIN2] transcription.


The [PROTEIN2] ald [/PROTEIN2] promoter, like the sigE promoter, is believed to be recognized by [PROTEIN1] sigmaA [/PROTEIN1] RNA polymerase, suggesting that sigmaK may inhibit sigmaA activity late in sporulation.


The ald promoter, like the [PROTEIN2] sigE [/PROTEIN2] promoter, is believed to be recognized by [PROTEIN1] sigmaA [/PROTEIN1] RNA polymerase, suggesting that sigmaK may inhibit sigmaA activity late in sporulation.


The ald promoter, like the sigE promoter, is believed to be recognized by [PROTEIN2] sigmaA [/PROTEIN2]RNA polymerase, suggesting that [PROTEIN1] sigmaK [/PROTEIN1] may inhibit sigmaA activity late in sporulation.


nsubjpass(regulated, expression); advmod(regulated, negatively)

In the mother cell compartment of sporulating cells, expression of the [PROTEIN2] sigE [/PROTEIN2] gene, encoding the earlier-acting sigma factor, sigmaE, is negatively regulated by the later-acting sigma factor, [PROTEIN1] sigmaK [/PROTEIN1].


The first stage, which involves the phosphatase function of [PROTEIN2] SpoIIE [/PROTEIN2], depends on the cell division protein [PROTEIN1] FtsZ [/PROTEIN1] and could correspond to the FtsZ-dependent assembly of SpoIIE into E-rings.


Evidence based on the use of modified and mutant forms of the phosphatase protein indicates that [PROTEIN1] SpoIIE [/PROTEIN1] blocks the capacity of unphosphorylated [PROTEIN2] SpoIIAA [/PROTEIN2] to activate sigmaF until formation of the polar septum is completed.


Evidence based on the use of modified and mutant forms of the phosphatase protein indicates that SpoIIE blocks the capacity of unphosphorylated [PROTEIN1] SpoIIAA [/PROTEIN1] to activate [PROTEIN2] sigmaF [/PROTEIN2] until formation of the polar septum is completed.


Cell-specific activation of transcription factor [PROTEIN2] sigmaF [/PROTEIN2]during sporulation in Bacillus subtilis requires the formation of the polar septum and the activity of a serine phosphatase ([PROTEIN1] SpoIIE [/PROTEIN1]) located in the septum.


The [PROTEIN1] SpoIIE [/PROTEIN1] phosphatase indirectly activates sigmaF by dephosphorylating a protein ([PROTEIN2] SpoIIAA-P [/PROTEIN2]) in the pathway that controls the activity of the transcription factor.


The [PROTEIN1] SpoIIE [/PROTEIN1] phosphatase indirectly activates [PROTEIN2] sigmaF [/PROTEIN2] by dephosphorylating a protein (SpoIIAA-P) in the pathway that controls the activity of the transcription factor.


The SpoIIE phosphatase indirectly activates [PROTEIN2] sigmaF [/PROTEIN2] by dephosphorylating a protein ([PROTEIN1] SpoIIAA-P [/PROTEIN1]) in the pathway that controls the activity of the transcription factor.


(i) The finding that the [PROTEIN2] bmrUR [/PROTEIN2] operon is under [PROTEIN1] sigmaB [/PROTEIN1] control indicates that the elimination of multidrug compounds might be a new function in multiple stress resistance.


The [PROTEIN1] ydaP [/PROTEIN1] gene might belong to the increasing number of [PROTEIN2] sigmaB [/PROTEIN2]-dependent genes whose orthologues are under the control of sigmas in Escherichia coli, indicating that both regulons may fulfil similar functions.


Three new [PROTEIN1] sigmaB [/PROTEIN1]-dependent genes ([PROTEIN2] ydaE [/PROTEIN2], ydaG and yfkM) encoding proteins with still unknown functions were also described.


Three new [PROTEIN1] sigmaB [/PROTEIN1]-dependent genes (ydaE, ydaG and [PROTEIN2] yfkM [/PROTEIN2]) encoding proteins with still unknown functions were also described.


Cell specificity is first established in the forespore under the control of the [PROTEIN2] sigma F [/PROTEIN2] factor, which is itself activated through the action of the [PROTEIN1] SpoIIE [/PROTEIN1] serine phosphatase, an enzyme targeted to the septum between the two cells.


Most [PROTEIN1] cot [/PROTEIN1] genes, and the gerE gene, are transcribed by [PROTEIN2] sigmaK [/PROTEIN2] RNA polymerase.


Most cot genes, and the [PROTEIN1] gerE [/PROTEIN1] gene, are transcribed by [PROTEIN2] sigmaK [/PROTEIN2] RNA polymerase.


Previously, it was shown that the [PROTEIN1] GerE [/PROTEIN1] protein inhibits transcription in vitro of the [PROTEIN2] sigK [/PROTEIN2] gene encoding sigmaK.


These results demonstrate that [PROTEIN1] sigmaK [/PROTEIN1]-dependent transcription of [PROTEIN2] gerE [/PROTEIN2] initiates a negative feedback loop in which GerE acts as a repressor to limit production of sigmaK.


acl(repressor, limit); dobj(limit, production)

These results demonstrate that sigmaK-dependent transcription of gerE initiates a negative feedback loop in which [PROTEIN1] GerE [/PROTEIN1] acts as a repressor to limit production of [PROTEIN2] sigmaK [/PROTEIN1].


A low level of [PROTEIN1] GerE [/PROTEIN1] activated transcription of cotD by [PROTEIN2] sigmaK [/PROTEIN2] RNA polymerase in vitro, but a higher level of GerE repressed cotD transcription.


activation of gene transcription by low level protein

A low level of GerE activated transcription of cotD by sigmaK RNA polymerase in vitro, but a higher level of [PROTEIN1] GerE [/PROTEIN1] repressed [PROTEIN2] cotD [/PROTEIN2] transcription.


A low level of GerE activated transcription of [PROTEIN2] cotD [/PROTEIN2] by [PROTEIN1] sigmaK [/PROTEIN1] RNA polymerase in vitro, but a higher level of GerE repressed cotD transcription.


negative regulation of gene transcription

Here, we show that [PROTEIN1] GerE [/PROTEIN1] binds near the [PROTEIN2] sigK [/PROTEIN2] transcriptional start site, to act as a repressor.


regulation of transcription by binding to promoter

We show that [PROTEIN1] GerE [/PROTEIN1] binds to two sites that span the -35 region of the [PROTEIN2] cotD [/PROTEIN2] promoter.


activate, transcription, repress, transcription

dobj(activate, transcription);  advmod(transcription, repress)

These results suggest that a rising level of [PROTEIN1] GerE [/PROTEIN1] in sporulating cells may first activate [PROTEIN2] cotD [/PROTEIN2] transcription from the upstream site then repress transcription as the downstream site becomes occupied.


[PROTEIN2] sspG [/PROTEIN2] transcription also requires the DNA binding protein [PROTEIN1] GerE [/PROTEIN1].


In contrast, [PROTEIN1] sspJ [/PROTEIN1] is transcribed in the forespore compartment by RNA polymerase with the forespore-specific [PROTEIN2] sigmaG [/PROTEIN2] and appears to give a monocistronic transcript.


positive regulation of gene transcription

[PROTEIN1] ComK [/PROTEIN1] negatively controls the transcription of hag by stimulating the transcription of comF-flgM, thereby increasing the production of the [PROTEIN2] FlgM [/PROTEIN2] antisigma factor that inhibits sigmaD activity.


dobj(controls, transcription); advmod(controls, negatively)

[PROTEIN1] ComK [/PROTEIN1] negatively controls the transcription of [PROTEIN2] hag [/PROTEIN2] by stimulating the transcription of comF-flgM, thereby increasing the production of the FlgM antisigma factor that inhibits sigmaD activity.


[PROTEIN1] ComK [/PROTEIN1] negatively controls the transcription of hag by stimulating the transcription of [PROTEIN2] comF [/PROTEIN2]-flgM, thereby increasing the production of the FlgM antisigma factor that inhibits sigmaD activity.


ComK negatively controls the transcription of hag by stimulating the transcription of comF-flgM, thereby increasing the production of the [PROTEIN1] FlgM [/PROTEIN1] antisigma factor that inhibits [PROTEIN2] sigmaD [/PROTEIN2] activity.


This stress-induced increase in [PROTEIN2] ykzA [/PROTEIN2] expression is absolutely dependent on the alternative sigma factor [PROTEIN1] sigmaB [/PROTEIN1], which controls a large stationary-phase and stress regulon.


[PROTEIN1] sigma X [/PROTEIN1] also contributes to the expression of [PROTEIN2] CsbB [/PROTEIN2], a putative membrane-bound glucosyl transferase that is partially controlled by the sigma B stress response sigma factor.


sigma X also contributes to the expression of [PROTEIN2] CsbB [/PROTEIN2], a putative membrane-bound glucosyl transferase that is partially controlled by the [PROTEIN1] sigma B [/PROTEIN1] stress response sigma factor.


Transcriptional studies showed that [PROTEIN2] nadE [/PROTEIN2] is strongly induced in response to heat, ethanol and salt stress or after starvation for glucose in a [PROTEIN1] sigma B [/PROTEIN1]-dependent manner.


Furthermore, [PROTEIN2] YtxH [/PROTEIN2] and YvyD seemed to be induced after phosphate starvation in the wild type in a [PROTEIN1] sigma(B) [/PROTEIN1]-dependent manner and in the sigB mutant probably via sigma(H).


Furthermore, YtxH and [PROTEIN1] YvyD [/PROTEIN1] seemed to be induced after phosphate starvation in the wild type in a [PROTEIN2] sigma(B) [/PROTEIN2]-dependent manner and in the sigB mutant probably via sigma(H).


Furthermore, [PROTEIN1] YtxH [/PROTEIN1] and YvyD seemed to be induced after phosphate starvation in the wild type in a sigma(B)-dependent manner and in the sigB mutant probably via [PROTEIN2] sigma(H) [/PROTEIN2].


Furthermore, YtxH and [PROTEIN2] YvyD [/PROTEIN2] seemed to be induced after phosphate starvation in the wild type in a sigma(B)-dependent manner and in the sigB mutant probably via [PROTEIN1] sigma(H) [/PROTEIN1].


From these results we conclude that [PROTEIN1] ComK [/PROTEIN1] negatively regulates degR expression by preventing [PROTEIN2] sigmaD [/PROTEIN2]-driven transcription of degR, possibly through interaction with the control region.


From these results we conclude that [PROTEIN1] ComK [/PROTEIN1] negatively regulates [PROTEIN2] degR [/PROTEIN2] expression by preventing sigmaD-driven transcription of degR, possibly through interaction with the control region.


From these results we conclude that ComK negatively regulates degR expression by preventing [PROTEIN1] sigmaD [/PROTEIN1]-driven transcription of [PROTEIN2] degR [/PROTEIN2], possibly through interaction with the control region.


We have shown previously that the transcription of [PROTEIN2] degR [/PROTEIN2] is driven by an alternative sigma factor, [PROTEIN1] sigmaD [/PROTEIN1].


DNase I footprinting showed that [PROTEIN1] SpoIIID [/PROTEIN1] binds strongly to two sites in the [PROTEIN2] cotC [/PROTEIN2] promoter region, binds weakly to one site in the cotX promoter, and does not bind specifically to cotB.


DNase I footprinting showed that [PROTEIN1] SpoIIID [/PROTEIN1] binds strongly to two sites in the cotC promoter region, binds weakly to one site in the [PROTEIN2] cotX [/PROTEIN2] promoter, and does not bind specifically to cotB.


DNase I footprinting showed that [PROTEIN1] SpoIIID [/PROTEIN1] binds strongly to two sites in the cotC promoter region, binds weakly to one site in the cotX promoter, and does not bind specifically to [PROTEIN2] cotB [/PROTEIN2].


Transcription of the [PROTEIN1] cotB [/PROTEIN1], cotC, and cotX genes by final [PROTEIN2] sigma(K) [/PROTEIN2] RNA polymerase is activated by a small, DNA-binding protein called GerE.


Transcription of the cotB, cotC, and [PROTEIN1] cotX [/PROTEIN1] genes by final [PROTEIN2] sigma(K) [/PROTEIN2] RNA polymerase is activated by a small, DNA-binding protein called GerE.


Transcription of the [PROTEIN2] cotB [/PROTEIN2], cotC, and cotX genes by final sigma(K) RNA polymerase is activated by a small, DNA-binding protein called [PROTEIN1] GerE [/PROTEIN1].


Transcription of the cotB, [PROTEIN2] cotC [/PROTEIN2], and cotX genes by final sigma(K) RNA polymerase is activated by a small, DNA-binding protein called [PROTEIN1] GerE [/PROTEIN1].


Transcription of the cotB, cotC, and [PROTEIN2] cotX [/PROTEIN2] genes by final sigma(K) RNA polymerase is activated by a small, DNA-binding protein called [PROTEIN1] GerE [/PROTEIN1].


In vitro transcription experiments suggest that the differential pattern of [PROTEIN2] cot [/PROTEIN2] gene expression results from the combined action of [PROTEIN1] GerE [/PROTEIN1] and another transcription factor, SpoIIID.


low concentration, activated, transcription

A low concentration of [PROTEIN1] GerE [/PROTEIN1] activated cotB transcription by final [PROTEIN2] sigma(K) [/PROTEIN2] RNA polymerase, whereas a higher concentration was needed to activate transcription of cotX or cotC.


A low concentration of [PROTEIN1] GerE [/PROTEIN1] activated [PROTEIN2] cotB [/PROTEIN2] transcription by final sigma(K) RNA polymerase, whereas a higher concentration was needed to activate transcription of cotX or cotC.


A low concentration of [PROTEIN1] GerE [/PROTEIN1] activated cotB transcription by final sigma(K) RNA polymerase, whereas a higher concentration was needed to activate transcription of [PROTEIN2] cotX [/PROTEIN2] or cotC.


A low concentration of GerE activated [PROTEIN2] cotB [/PROTEIN2] transcription by final [PROTEIN1] sigma(K) [/PROTEIN1] RNA polymerase, whereas a higher concentration was needed to activate transcription of cotX or cotC.


[PROTEIN1] SpoIIID [/PROTEIN1] at low concentration repressed [PROTEIN2] cotC [/PROTEIN2] transcription, whereas a higher concentration only partially repressed cotX transcription and had little effect on cotB transcription.


[PROTEIN1] SpoIIID [/PROTEIN1] at low concentration repressed cotC transcription, whereas a higher concentration only partially repressed [PROTEIN2] cotX [/PROTEIN2] transcription and had little effect on cotB transcription.


[PROTEIN1] SpoIIID [/PROTEIN1] at low concentration repressed cotC transcription, whereas a higher concentration only partially repressed cotX transcription and had little effect on [PROTEIN2] cotB [/PROTEIN2] transcription.


Primer extension experiments and Northern blot analysis show that an active [PROTEIN1] sigmaA [/PROTEIN1]-dependent promoter precedes [PROTEIN2] kdgR [/PROTEIN2] and transcription is terminated at the putative p-independent terminator downstream of kdgT.


A [PROTEIN1] sigmaW [/PROTEIN1]-dependent promoter (PW) precedes [PROTEIN2] sigW [/PROTEIN2], demonstrating that this transcription factor is positively autoregulated.


We overproduced and purified sigma(X) from Escherichia coli and demonstrate that in vitro, both [PROTEIN1] sigma(A) [/PROTEIN1] and sigma(X) holoenzymes recognize promoter elements within the [PROTEIN2] sigX [/PROTEIN2]-ypuN control region.


We overproduced and purified sigma(X) from Escherichia coli and demonstrate that in vitro, both [PROTEIN1] sigma(A) [/PROTEIN1] and sigma(X) holoenzymes recognize promoter elements within the sigX-[PROTEIN2] ypuN [/PROTEIN2] control region.


We overproduced and purified [PROTEIN1] sigma(X) [/PROTEIN1] from Escherichia coli and demonstrate that in vitro, both sigma(A) and sigma(X) holoenzymes recognize promoter elements within the [PROTEIN2] sigX [/PROTEIN2]-ypuN control region.


The results indicate that [PROTEIN1] PhoP~P [/PROTEIN1] is sufficient to repress the transcription of the [PROTEIN2] tagA [/PROTEIN2] and tagD promoters and also to activate the transcription of the tuaA promoter.


The results indicate that [PROTEIN1] PhoP~P [/PROTEIN1] is sufficient to repress the transcription of the tagA and [PROTEIN2] tagD [/PROTEIN2] promoters and also to activate the transcription of the tuaA promoter.


The results indicate that [PROTEIN1] PhoP~P [/PROTEIN1] is sufficient to repress the transcription of the tagA and tagD promoters and also to activate the transcription of the [PROTEIN2] tuaA [/PROTEIN2] promoter.


expression, promoter, negatively regulated

negative regulation of transcription by binding to promoter

Transcriptional studies demonstrated that the expression from the [PROTEIN2] araE [/PROTEIN2] promoter is induced by L-arabinose, repressed by glucose, and negatively regulated by [PROTEIN1] AraR [/PROTEIN1].


positive regulation of transcription by binding to promoter

During endospore formation in Bacillus subtilis, the DNA binding protein [PROTEIN2] GerE [/PROTEIN2] stimulates transcription from several promoters that are used by RNA polymerase containing [PROTEIN1] sigmaK [/PROTEIN1]


[PROTEIN1] GerE [/PROTEIN1] binds to a site on one of these promoters, [PROTEIN2] cotX [/PROTEIN2], that overlaps its -35 region.


However, the mutant was unable to stimulate transcription by final [PROTEIN2] sigma(A) [/PROTEIN2]-RNA polymerase from the [PROTEIN1] Spo0A [/PROTEIN1]-dependent spoIIG operon promoter.


However, the mutant was unable to stimulate transcription by final sigma(A)-RNA polymerase from the [PROTEIN1] Spo0A [/PROTEIN1]-dependent [PROTEIN2] spoIIG [/PROTEIN2] operon promoter.


However, the mutant was unable to stimulate transcription by final [PROTEIN1] sigma(A) [/PROTEIN1]-RNA polymerase from the Spo0A-dependent [PROTEIN2] spoIIG [/PROTEIN2] operon promoter.


The Bacillus subtilis [PROTEIN2] clpC [/PROTEIN2] operon is regulated by two stress induction pathways relying on either [PROTEIN1] sigmaB [/PROTEIN1] or a class III stress induction mechanism acting at a sigmaA-like promoter.


The Bacillus subtilis [PROTEIN2] clpC [/PROTEIN2] operon is regulated by two stress induction pathways relying on either sigmaB or a class III stress induction mechanism acting at a [PROTEIN1] sigmaA [/PROTEIN1]-like promoter.


Our data demonstrate that the [PROTEIN1] CtsR [/PROTEIN1] protein acts as a global repressor of the [PROTEIN2] clpC [/PROTEIN2] operon, as well as other class III heat shock genes, by preventing unstressed transcription from either the sigmaB- or sigmaA-dependent promoter and might be inactivated or dissociate under inducing stress conditions.


Our data demonstrate that the CtsR protein acts as a global repressor of the [PROTEIN2] clpC [/PROTEIN2] operon, as well as other class III heat shock genes, by preventing unstressed transcription from either the [PROTEIN1] sigmaB [/PROTEIN1]- or sigmaA-dependent promoter and might be inactivated or dissociate under inducing stress conditions.


Our data demonstrate that the CtsR protein acts as a global repressor of the [PROTEIN2] clpC [/PROTEIN2] operon, as well as other class III heat shock genes, by preventing unstressed transcription from either the sigmaB- or [PROTEIN2] sigmaA [/PROTEIN2]-dependent promoter and might be inactivated or dissociate under inducing stress conditions.


The [PROTEIN1] sigmaB [/PROTEIN1]-dependent promoter drives expression of [PROTEIN2] yvyD [/PROTEIN2] under stress conditions and after glucose starvation, whereas a sigmaH-dependent promoter is responsible for yvyD transcription following amino acid limitation.


This indicates that the [PROTEIN2] yvyD [/PROTEIN2] gene product, being a member of both the sigmaB and [PROTEIN1] sigmaH [/PROTEIN1] regulons, might negatively regulate the activity of the sigmaL regulon.


This indicates that the [PROTEIN1] yvyD [/PROTEIN1] gene product, being a member of both the sigmaB and sigmaH regulons, might negatively regulate the activity of the [PROTEIN2] sigmaL [/PROTEIN2] regulon.


Therefore, ftsY is solely expressed during sporulation from a [PROTEIN1] sigma(K) [/PROTEIN1]- and GerE-controlled promoter that is located immediately upstream of [PROTEIN2] ftsY [/PROTEIN2] inside the smc gene.


Therefore, [PROTEIN2] ftsY [/PROTEIN2] is solely expressed during sporulation from a sigma(K)- and [PROTEIN1] GerE [/PROTEIN1]-controlled promoter that is located immediately upstream of ftsY inside the smc gene.


In that respect sigB is similar to the previously described gene [PROTEIN2] gsiB [/PROTEIN2] which is also a member of the [PROTEIN1] sigmaB [/PROTEIN1] regulon.


In that respect [PROTEIN2] sigB [/PROTEIN2] is similar to the previously described gene gsiB which is also a member of the [PROTEIN1] sigmaB [/PROTEIN1] regulon.


The addition of [PROTEIN1] ClpX [/PROTEIN1] to in vitro transcription reactions resulted in the stimulation of RNAP holoenzyme activity, but [PROTEIN2] sigmaH [/PROTEIN2]-RNAP was observed to be more sensitive to ClpX-dependent stimulation than sigmaA-RNAP.


The addition of ClpX to in vitro transcription reactions resulted in the stimulation of RNAP holoenzyme activity, but sigmaH-RNAP was observed to be more sensitive to [PROTEIN1] ClpX [/PROTEIN1]-dependent stimulation than [PROTEIN2] sigmaA [/PROTEIN2]-RNAP.


The addition of ClpX to in vitro transcription reactions resulted in the stimulation of RNAP holoenzyme activity, but [PROTEIN2] sigmaH [/PROTEIN2]-RNAP was observed to be more sensitive to [PROTEIN1] ClpX [/PROTEIN1]-dependent stimulation than sigmaA-RNAP.


The addition of [PROTEIN1] ClpX [/PROTEIN1] to in vitro transcription reactions resulted in the stimulation of RNAP holoenzyme activity, but sigmaH-RNAP was observed to be more sensitive to ClpX-dependent stimulation than [PROTEIN2] sigmaA [/PROTEIN2]-RNAP.


Although [PROTEIN2] spo0H [/PROTEIN2] is transcriptionally regulated by the key regulatory device that controls sporulation initiation, the [PROTEIN1] Spo0 [/PROTEIN1] phosphorelay, there is considerable evidence implicating a mechanism of post-translational control that governs the activity and concentration of sigmaH.


The class includes AsiA form bacteriophage T4, which inhibits Escherichia coli sigma 70; FlgM, present in both gram-positive and gram-negative bacteria, which inhibits the flagella sigma factor sigma 28; [PROTEIN1] SpoIIAB [/PROTEIN1], which inhibits the sporulation-specific sigma factor, sigma F and [PROTEIN2] sigma G [/PROTEIN2], of Bacillus subtilis; RbsW of B. subtilis, which inhibits stress response sigma factor sigma B; and DnaK, a general regulator of the heat shock response, which in bacteria inhibits the heat shock sigma factor sigma 32.


The class includes AsiA form bacteriophage T4, which inhibits Escherichia coli sigma 70; [PROTEIN1] FlgM [/PROTEIN1], present in both gram-positive and gram-negative bacteria, which inhibits the flagella sigma factor [PROTEIN2] sigma 28 [/PROTEIN2]; SpoIIAB, which inhibits the sporulation-specific sigma factor, sigma F and sigma G, of Bacillus subtilis; RbsW of B. subtilis, which inhibits stress response sigma factor sigma B; and DnaK, a general regulator of the heat shock response, which in bacteria inhibits the heat shock sigma factor sigma 32.


The class includes AsiA form bacteriophage T4, which inhibits Escherichia coli sigma 70; FlgM, present in both gram-positive and gram-negative bacteria, which inhibits the flagella sigma factor sigma 28; SpoIIAB, which inhibits the sporulation-specific sigma factor, sigma F and sigma G, of Bacillus subtilis; [PROTEIN1] RbsW [/PROTEIN1] of B. subtilis, which inhibits stress response sigma factor [PROTEIN2] sigma B [/PROTEIN2]; and DnaK, a general regulator of the heat shock response, which in bacteria inhibits the heat shock sigma factor sigma 32.


The class includes AsiA form bacteriophage T4, which inhibits Escherichia coli sigma 70; FlgM, present in both gram-positive and gram-negative bacteria, which inhibits the flagella sigma factor sigma 28; SpoIIAB, which inhibits the sporulation-specific sigma factor, sigma F and sigma G, of Bacillus subtilis; RbsW of B. subtilis, which inhibits stress response sigma factor sigma B; and [PROTEIN1] DnaK [/PROTEIN1], a general regulator of the heat shock response, which in bacteria inhibits the heat shock sigma factor [PROTEIN2] sigma 32 [/PROTEIN2].


Finally, we show that proper localization of [PROTEIN2] SpoIVA [/PROTEIN2] required the expression of one or more genes which, like spoIVA, are under the control of the mother cell transcription factor [PROTEIN1] sigmaE [/PROTEIN1].


The [PROTEIN2] sspH [/PROTEIN2]and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, [PROTEIN1] sigmaG [/PROTEIN1]; the sspN-tlp operon is recognized equally well by sigmaG and the other forespore-specific sigma factor, sigmaF.


The sspH and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, sigmaG; the [PROTEIN2] sspN [/PROTEIN2]-tlp operon is recognized equally well by [PROTEIN1] sigmaG [/PROTEIN1] and the other forespore-specific sigma factor, sigmaF.


The sspH and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, sigmaG; the sspN-[PROTEIN2] tlp [/PROTEIN2] operon is recognized equally well by [PROTEIN1] sigmaG [/PROTEIN1] and the other forespore-specific sigma factor, sigmaF.


The sspH and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, sigmaG; the [PROTEIN2] sspN [/PROTEIN2]-tlp operon is recognized equally well by sigmaG and the other forespore-specific sigma factor, [PROTEIN1] sigmaF [/PROTEIN1].


The sspH and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, sigmaG; the sspN-[PROTEIN2] tlp [/PROTEIN2] operon is recognized equally well by sigmaG and the other forespore-specific sigma factor, [PROTEIN1] sigmaF [/PROTEIN1].


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase ([PROTEIN2] RacX [/PROTEIN2]), homologues of signal peptide peptidase (YteI), flotillin (YuaG), ABC transporters (YknXYZ), non-haem bromoperoxidase (YdjP), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides.


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase ([PROTEIN2] YteI [/PROTEIN2]), flotillin (YuaG), ABC transporters (YknXYZ), non-haem bromoperoxidase (YdjP), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides.


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase (YteI), flotillin ([PROTEIN2] YuaG [/PROTEIN2]), ABC transporters (YknXYZ), non-haem bromoperoxidase (YdjP), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides.


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase (YteI), flotillin (YuaG), ABC transporters ([PROTEIN2] YknXYZ [/PROTEIN2]), non-haem bromoperoxidase (YdjP), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides.


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase (YteI), flotillin (YuaG), ABC transporters (YknXYZ), non-haem bromoperoxidase ([PROTEIN2] YdjP [/PROTEIN2]), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides.


The [PROTEIN1] sigma W [/PROTEIN1] regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase (YteI), flotillin (YuaG), ABC transporters (YknXYZ), non-haem bromoperoxidase (YdjP), epoxide hydrolase ([PROTEIN2] YfhM [/PROTEIN2]) and three small peptides with structural similarities to bacteriocin precursor polypeptides.