Publication Information
Finkemeier et al., 2011
No external accession available
Abstract
Plant Physiol. 2011 Apr;155(4):1779-90. doi: 10.1104/pp.110.171595. Epub 2011
Feb 10.
Proteins of diverse function and subcellular location are lysine acetylated in
Arabidopsis.
Finkemeier I(1), Laxa M, Miguet L, Howden AJ, Sweetlove LJ.
Author information:
(1)Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United
Kingdom.
Acetylation of the ε-amino group of lysine (Lys) is a reversible
posttranslational modification recently discovered to be widespread, occurring
on proteins outside the nucleus, in most subcellular locations in mammalian
cells. Almost nothing is known about this modification in plants beyond the
well-studied acetylation of histone proteins in the nucleus. Here, we report
that Lys acetylation in plants also occurs on organellar and cytosolic proteins.
We identified 91 Lys-acetylated sites on 74 proteins of diverse functional
classes. Furthermore, our study suggests that Lys acetylation may be an
important posttranslational modification in the chloroplast, since four Calvin
cycle enzymes were acetylated. The plastid-encoded large subunit of Rubisco
stands out because of the large number of acetylated sites occurring at
important Lys residues that are involved in Rubisco tertiary structure formation
and catalytic function. Using the human recombinant deacetylase sirtuin 3, it
was demonstrated that Lys deacetylation significantly affects Rubisco activity
as well as the activities of other central metabolic enzymes, such as the Calvin
cycle enzyme phosphoglycerate kinase, the glycolytic enzyme glyceraldehyde
3-phosphate dehydrogenase, and the tricarboxylic acid cycle enzyme malate
dehydrogenase. Our results demonstrate that Lys acetylation also occurs on
proteins outside the nucleus in Arabidopsis (Arabidopsis thaliana) and that Lys
acetylation could be important in the regulation of key metabolic enzymes.
DOI: 10.1104/pp.110.171595
PMCID: PMC3091095
PMID: 21311031 [Indexed for MEDLINE]
