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פותח על ידי קלירמאש פתרונות בע"מ -
Acetylation represses the binding of CheY to its target proteins
Year:
2010
Source of publication :
Molecular Microbiology
Authors :
ליארזי, אורנה
;
.
Volume :
76
Co-Authors:
Liarzi, O., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Barak, R., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Bronner, V., Bio-Rad Haifa, 32000 Haifa, Israel
Dines, M., Bio-Rad Haifa, 32000 Haifa, Israel, Department of Neurobiology and Ethology, Faculty of Science and Science Education, University of Haifa, Mt. Carmel 31905, Israel
Sagi, Y., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel, Department of Medicine, Division of Oncology, Stanford University School of Medicine, Stanford, CA 94305, United States
Shainskaya, A., Biological Mass Spectrometry Facility, Department of Biological Services, Weizmann Institute of Science, 76100 Rehovot, Israel
Eisenbach, M., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Facilitators :
From page:
932
To page:
943
(
Total pages:
12
)
Abstract:
The ability of CheY, the response regulator of bacterial chemotaxis, to generate clockwise rotation is regulated by two covalent modifications - phosphorylation and acetylation. While the function and signal propagation of the former are widely understood, the mechanism and role of the latter are still obscure. To obtain information on the function of this acetylation, we non-enzymatically acetylated CheY to a level similar to that found in vivo, and examined its binding to its kinase CheA, its phosphatase CheZ and the switch protein FliM - its target at the flagellar switch complex. Acetylation repressed the binding to all three proteins. These results suggest that both phosphorylation and acetylation determine CheY's ability to bind to its target proteins, thus providing two levels of regulation, fast and slow respectively. The fast level is modulated by environmental signals (e.g. chemotactic and thermotactic stimuli). The slow one is regulated by the metabolic state of the cell and it determines, at each metabolic state, the fraction of CheY molecules that can participate in signalling. © 2010 Blackwell Publishing Ltd.
Note:
Related Files :
Genetics
metabolism
molecular genetics
Molecular Sequence Data
signal transduction
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1111/j.1365-2958.2010.07148.x
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19704
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:31
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Scientific Publication
Acetylation represses the binding of CheY to its target proteins
76
Liarzi, O., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Barak, R., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Bronner, V., Bio-Rad Haifa, 32000 Haifa, Israel
Dines, M., Bio-Rad Haifa, 32000 Haifa, Israel, Department of Neurobiology and Ethology, Faculty of Science and Science Education, University of Haifa, Mt. Carmel 31905, Israel
Sagi, Y., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel, Department of Medicine, Division of Oncology, Stanford University School of Medicine, Stanford, CA 94305, United States
Shainskaya, A., Biological Mass Spectrometry Facility, Department of Biological Services, Weizmann Institute of Science, 76100 Rehovot, Israel
Eisenbach, M., Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel
Acetylation represses the binding of CheY to its target proteins
The ability of CheY, the response regulator of bacterial chemotaxis, to generate clockwise rotation is regulated by two covalent modifications - phosphorylation and acetylation. While the function and signal propagation of the former are widely understood, the mechanism and role of the latter are still obscure. To obtain information on the function of this acetylation, we non-enzymatically acetylated CheY to a level similar to that found in vivo, and examined its binding to its kinase CheA, its phosphatase CheZ and the switch protein FliM - its target at the flagellar switch complex. Acetylation repressed the binding to all three proteins. These results suggest that both phosphorylation and acetylation determine CheY's ability to bind to its target proteins, thus providing two levels of regulation, fast and slow respectively. The fast level is modulated by environmental signals (e.g. chemotactic and thermotactic stimuli). The slow one is regulated by the metabolic state of the cell and it determines, at each metabolic state, the fraction of CheY molecules that can participate in signalling. © 2010 Blackwell Publishing Ltd.
Scientific Publication
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