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Proc Natl Acad Sci U S A. 2018 Jan 2;115(1):210-215. doi: 10.1073/pnas.1717519115. Epub 2017 Dec 19.

Fungal-induced protein hyperacetylation in maize identified by acetylome profiling.

Author information

1
Department of Plant Pathology and Microbiology, Iowa State University, Ames, IA 50011; jwalley@iastate.edu sbriggs@ucsd.edu.
2
Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
3
Department of Plant Pathology and Microbiology, Iowa State University, Ames, IA 50011.
4
Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093 jwalley@iastate.edu sbriggs@ucsd.edu.

Abstract

Lysine acetylation is a key posttranslational modification that regulates diverse proteins involved in a range of biological processes. The role of histone acetylation in plant defense is well established, and it is known that pathogen effector proteins encoding acetyltransferases can directly acetylate host proteins to alter immunity. However, it is unclear whether endogenous plant enzymes can modulate protein acetylation during an immune response. Here, we investigate how the effector molecule HC-toxin (HCT), a histone deacetylase inhibitor produced by the fungal pathogen Cochliobolus carbonum race 1, promotes virulence in maize through altering protein acetylation. Using mass spectrometry, we globally quantified the abundance of 3,636 proteins and the levels of acetylation at 2,791 sites in maize plants treated with HCT as well as HCT-deficient or HCT-producing strains of C. carbonum Analyses of these data demonstrate that acetylation is a widespread posttranslational modification impacting proteins encoded by many intensively studied maize genes. Furthermore, the application of exogenous HCT enabled us to show that the activity of plant-encoded enzymes (histone deacetylases) can be modulated to alter acetylation of nonhistone proteins during an immune response. Collectively, these results provide a resource for further mechanistic studies examining the regulation of protein function by reversible acetylation and offer insight into the complex immune response triggered by virulent C. carbonum.

KEYWORDS:

acetylome; immunity; maize; proteome

PMID:
29259121
PMCID:
PMC5776827
DOI:
10.1073/pnas.1717519115
[Indexed for MEDLINE]
Free PMC Article

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