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פותח על ידי קלירמאש פתרונות בע"מ -
In Vivo Acetylation of CheY, a Response Regulator in Chemotaxis of Escherichia coli
Year:
2008
Source of publication :
Journal of Molecular Biology
Authors :
ליארזי, אורנה
;
.
Volume :
376
Co-Authors:
Yan, J., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Barak, R., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Liarzi, O., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Shainskaya, A., Biological Mass Spectrometry Facility, Department of Biological Services, The Weizmann Institute of Science, 76100 Rehovot, Israel
Eisenbach, M., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Facilitators :
From page:
1260
To page:
1271
(
Total pages:
12
)
Abstract:
CheY, the excitatory response regulator in the chemotaxis system of Escherichia coli, can be modulated by two covalent modifications: phosphorylation and acetylation. Both modifications have been detected in vitro only. The role of CheY acetylation is still obscure, although it is known to be involved in chemotaxis and to occur in vitro by two mechanisms-acetyl-CoA synthetase-catalyzed transfer of acetyl groups from acetate to CheY and autocatalyzed transfer from AcCoA. Here, we succeeded in detecting CheY acetylation in vivo by three means-Western blotting with a specific anti-acetyl-lysine antibody, mass spectrometry, and radiolabeling with [ 14C]acetate in the presence of protein-synthesis inhibitor. Unexpectedly, the level and rate of CheY acetylation in vivo were much higher than that in vitro. Thus, before any treatment, 9-13% of the lysine residues were found acetylated, depending on the growth phase, meaning that, on average, essentially every CheY molecule was acetylated in vivo. This high level was mainly the outcome of autoacetylation. Addition of acetate caused an incremental increase in the acetylation level, in which acetyl-CoA synthetase was involved too. These findings may have far-reaching implications for the structure-function relationship of CheY. © 2007 Elsevier Ltd. All rights reserved.
Note:
Related Files :
acetic acid c 14
acetyl coenzyme A synthetase
bacterial chemotaxis
in vivo study
Membrane Proteins
protein synthesis
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.jmb.2007.12.070
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19813
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:31
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Scientific Publication
In Vivo Acetylation of CheY, a Response Regulator in Chemotaxis of Escherichia coli
376
Yan, J., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Barak, R., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Liarzi, O., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
Shainskaya, A., Biological Mass Spectrometry Facility, Department of Biological Services, The Weizmann Institute of Science, 76100 Rehovot, Israel
Eisenbach, M., Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel
In Vivo Acetylation of CheY, a Response Regulator in Chemotaxis of Escherichia coli
CheY, the excitatory response regulator in the chemotaxis system of Escherichia coli, can be modulated by two covalent modifications: phosphorylation and acetylation. Both modifications have been detected in vitro only. The role of CheY acetylation is still obscure, although it is known to be involved in chemotaxis and to occur in vitro by two mechanisms-acetyl-CoA synthetase-catalyzed transfer of acetyl groups from acetate to CheY and autocatalyzed transfer from AcCoA. Here, we succeeded in detecting CheY acetylation in vivo by three means-Western blotting with a specific anti-acetyl-lysine antibody, mass spectrometry, and radiolabeling with [ 14C]acetate in the presence of protein-synthesis inhibitor. Unexpectedly, the level and rate of CheY acetylation in vivo were much higher than that in vitro. Thus, before any treatment, 9-13% of the lysine residues were found acetylated, depending on the growth phase, meaning that, on average, essentially every CheY molecule was acetylated in vivo. This high level was mainly the outcome of autoacetylation. Addition of acetate caused an incremental increase in the acetylation level, in which acetyl-CoA synthetase was involved too. These findings may have far-reaching implications for the structure-function relationship of CheY. © 2007 Elsevier Ltd. All rights reserved.
Scientific Publication
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