Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae
The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcr...
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| Autor*in: |
Crawford, J. Adam [verfasserIn] Kaper, James B. [verfasserIn] DiRita, Victor J. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford BSL: Blackwell Science Ltd, UK ; 1998 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 29(1998), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:29 ; year:1998 ; number:1 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1046/j.1365-2958.1998.00925.x |
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| 520 | |a The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. | ||
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10.1046/j.1365-2958.1998.00925.x doi (DE-627)NLEJ243577672 DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae Oxford BSL Blackwell Science Ltd, UK 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut DiRita, Victor J. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 29(1998), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:29 year:1998 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1998 1 0 |
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10.1046/j.1365-2958.1998.00925.x doi (DE-627)NLEJ243577672 DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae Oxford BSL Blackwell Science Ltd, UK 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut DiRita, Victor J. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 29(1998), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:29 year:1998 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1998 1 0 |
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10.1046/j.1365-2958.1998.00925.x doi (DE-627)NLEJ243577672 DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae Oxford BSL Blackwell Science Ltd, UK 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut DiRita, Victor J. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 29(1998), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:29 year:1998 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1998 1 0 |
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10.1046/j.1365-2958.1998.00925.x doi (DE-627)NLEJ243577672 DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae Oxford BSL Blackwell Science Ltd, UK 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut DiRita, Victor J. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 29(1998), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:29 year:1998 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1998 1 0 |
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10.1046/j.1365-2958.1998.00925.x doi (DE-627)NLEJ243577672 DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae Oxford BSL Blackwell Science Ltd, UK 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut DiRita, Victor J. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 29(1998), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:29 year:1998 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1998 1 0 |
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Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae |
| abstract |
The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. |
| abstractGer |
The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. |
| abstract_unstemmed |
The membrane proteins ToxR and ToxS regulate a variety of genes associated with the virulence of Vibrio cholerae, the agent of human cholera. One of the ToxRS-regulated genes is the ompU gene, which encodes a porin that may also act as an adhesin. To begin to understand the mechanism of ompU transcription activation by ToxRS, we performed genetic and biochemical studies on the ompU promoter. Deletions with a 5′ end-point at or downstream of −128, relative to the start site for transcription, did not direct expression of a lacZ reporter gene in wild-type V. cholerae, although the −128 promoter fragment did direct ToxRS-dependent reporter gene activity under conditions of ToxR overexpression in E. coli. Consistent with the activation data is that membranes containing ToxR and ToxS caused a gel electrophoretic mobility shift when mixed at low concentrations with deletion fragments whose end-point is at −211, but not with −128 or −68 fragments. ToxRS membranes did shift the −128 fragment when added at higher concentrations. DNase I footprinting analysis of ompU promoter DNA complexed with ToxRS membranes demonstrated protection of three sites: an upstream site ranging from −238 to −139, and two downstream sites ranging from −116 to −58 and −53 to −24. Within the DNA protected from DNase I digestion by ToxRS membranes, there are no elements bearing similarity to those identified previously within the promoters of two other ToxR-dependent genes, ctxA and toxT. We suggest a model for transcription activation that involves sequential ToxR-binding events to distinct regions in the ompU promoter. |
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| title_short |
Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae |
| url |
http://dx.doi.org/10.1046/j.1365-2958.1998.00925.x |
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| author2 |
Kaper, James B. DiRita, Victor J. |
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Kaper, James B. DiRita, Victor J. |
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| doi_str |
10.1046/j.1365-2958.1998.00925.x |
| up_date |
2024-07-06T05:54:40.606Z |
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| score |
7.401967 |