Publication Information
Wu et al., 2011
No external accession available
Abstract
Plant Physiol. 2011 Apr;155(4):1769-78. doi: 10.1104/pp.110.165852. Epub 2011
Feb 10.
Lysine acetylation is a widespread protein modification for diverse proteins in
Arabidopsis.
Wu X(1), Oh MH, Schwarz EM, Larue CT, Sivaguru M, Imai BS, Yau PM, Ort DR, Huber
SC.
Author information:
(1)Program in Physiological and Molecular Plant Biology , University of
Illinois, Urbana, Illinois 61801, USA.
Lysine acetylation (LysAc), a form of reversible protein posttranslational
modification previously known only for histone regulation in plants, is shown to
be widespread in Arabidopsis (Arabidopsis thaliana). Sixty-four Lys modification
sites were identified on 57 proteins, which operate in a wide variety of
pathways/processes and are located in various cellular compartments. A number of
photosynthesis-related proteins are among this group of LysAc proteins,
including photosystem II (PSII) subunits, light-harvesting chlorophyll
a/b-binding proteins (LHCb), Rubisco large and small subunits, and chloroplastic
ATP synthase (β-subunit). Using two-dimensional native green/sodium dodecyl
sulfate gels, the loosely PSII-bound LHCb was separated from the LHCb that is
tightly bound to PSII and shown to have substantially higher level of LysAc,
implying that LysAc may play a role in distributing the LHCb complexes. Several
potential LysAc sites were identified on eukaryotic elongation factor-1A
(eEF-1A) by liquid chromatography/mass spectrometry and using sequence- and
modification-specific antibodies the acetylation of Lys-227 and Lys-306 was
established. Lys-306 is contained within a predicted calmodulin-binding sequence
and acetylation of Lys-306 strongly inhibited the interactions of eEF-1A
synthetic peptides with calmodulin recombinant proteins in vitro. These results
suggest that LysAc of eEF-1A may directly affect regulatory properties and
localization of the protein within the cell. Overall, these findings reveal the
possibility that reversible LysAc may be an important and previously unknown
regulatory mechanism of a large number of nonhistone proteins affecting a wide
range of pathways and processes in Arabidopsis and likely in all plants.
DOI: 10.1104/pp.110.165852
PMCID: PMC3091122
PMID: 21311030 [Indexed for MEDLINE]
