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Bacillus subtilisSa...
Bacillus subtilisSalA is a phosphorylation-dependent transcription regulator that represses scoC and activates the production of the exoprotease AprE
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- Derouiche, Abderahmane, 1980 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Shi, Lei, 1981 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Bidnenko, V. (författare)
- Microbiologie de l'Alimentation au Service de la Sante Humaine
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- Ventroux, M. (författare)
- Microbiologie de l'Alimentation au Service de la Sante Humaine
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- Pigonneau, N. (författare)
- Microbiologie de l'Alimentation au Service de la Sante Humaine
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- Franz-Wachtel, M. (författare)
- Eberhard Karls Universität Tübingen,Eberhard Karls University of Tübingen
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- Kalantari, Aida, 1986 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Nessler, S. (författare)
- Université Paris-Sud XI,University of Paris-Sud XI
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- Noirot-Gros, M. F. (författare)
- Microbiologie de l'Alimentation au Service de la Sante Humaine
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- Mijakovic, Ivan, 1975 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- 2015-07-17
- 2015
- Engelska.
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Ingår i: Molecular Microbiology. - : Wiley. - 1365-2958 .- 0950-382X. ; 97:6, s. 1195-1208
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Abstract
Ämnesord
Stäng
- Bacillus subtilisMrp family protein SalA has been shown to indirectly promote the production of the exoprotease AprE by inhibiting the expression of scoC, which codes for a repressor of aprE. The exact mechanism by which SalA influences scoC expression has not been clarified previously. We demonstrate that SalA possesses a DNA-binding domain (residues 1-60), which binds to the promoter region of scoC. The binding of SalA to its target DNA depends on the presence of ATP and is stimulated by phosphorylation of SalA at tyrosine 327. The B.subtilis protein-tyrosine kinase PtkA interacts specifically with the C-terminal domain of SalAin vivo and in vitro and is responsible for activating its DNA binding via phosphorylation of tyrosine 327. In vivo, a mutant mimicking phosphorylation of SalA (SalA Y327E) exhibited a strong repression of scoC and consequently overproduction of AprE. By contrast, the non-phosphorylatable SalA Y327F and the ΔptkA exhibited the opposite effect, stronger expression of scoC and lower production of the exoprotease. Interestingly, both SalA and PtkA contain the same ATP-binding Walker domain and have thus presumably arisen from the common ancestral protein. Their regulatory interplay seems to be conserved in other bacteria.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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Till lärosätets databas
- Av författaren/redakt...
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Derouiche, Abder ...
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Shi, Lei, 1981
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Bidnenko, V.
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Ventroux, M.
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Pigonneau, N.
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Franz-Wachtel, M ...
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visa fler...
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Kalantari, Aida, ...
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Nessler, S.
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Noirot-Gros, M. ...
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Mijakovic, Ivan, ...
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visa färre...
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
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Molecular Microb ...
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Chalmers tekniska högskola