Publication:
The protein acetyltransferase PatZ from Escherichia coli is regulated by autoacetylation-induced oligomerization

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J.Biol.Che..5.pdf(1.89 MB)
Date
2015
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Authors
Castaño Cerezo, Sara ; Bernal Sanchez, Vicente ; Manjón Rubio, Antonio ; Fernández Espín, Vanesa ; García de la Torre, José ; Cánovas Díaz, Manuel ; Diego Puente, Teresa de ; Gallego Jara, Julia
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Bioquímica y Biología Molecular B e Inmunología
DOI
http://www.jbc.org/cgi/doi/10.1074/jbc.M115.649806
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info:eu-repo/semantics/article
Description
©2015. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the Accepted version of a Published Work that appeared in final form in Journal of Biological Chemistry (JBC). To access the final edited and published work see http://www.jbc.org/cgi/doi/10.1074/jbc.M115.649806
Abstract
Background: PatZ is the main Escherichia coli acetyltransferase and control acetyl-CoA synthetase (Acs) activity. Results: The kinetic and structural PatZ oligomer characteristics were determined. Conclusion: PatZ is a stable tetramer and forms an active octamer by autoacetylation to increase its stability. Significance: PTMs by acetylation have structural and functional roles in the cell.
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Acetyltransferase , Post-translational modification (PTM) , Acetyl coenzyme A (acetyl-CoA) , Escherichia coli (E. coli) , Lysine acetylation , Autoacetylation , Oligomerization , Protein acetyltransferase (PatZ or YfiQ)
Citation
Journal of Biological Chemistry (JBC)
URI
http://hdl.handle.net/10201/136586
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