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dc.contributor.author
Uhrig, R. Glen
dc.contributor.author
Schläpfer, Pascal
dc.contributor.author
Mehta, Devang
dc.contributor.author
Hirsch-Hoffmann, Matthias
dc.contributor.author
Gruissem, Wilhelm
dc.date.accessioned
2017-12-06T08:59:09Z
dc.date.available
2017-10-06T02:22:30Z
dc.date.available
2017-12-06T08:59:09Z
dc.date.issued
2017-07-05
dc.identifier.other
10.1186/s12864-017-3894-0
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/190698
dc.identifier.doi
10.3929/ethz-b-000190698
dc.description.abstract
Background Reversible protein acetylation occurring on Lys-Ne has emerged as a key regulatory post-translational modification in eukaryotes. It is mediated by two groups of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (KDACs) that catalyze the addition and removal of acetyl groups from target proteins. Estimates indicate that protein acetylation is second to protein phosphorylation in abundance, with thousands of acetylated sites now identified in different subcellular compartments. Considering the important regulatory role of protein phosphorylation, elucidating the diversity of KATs and KDACs across photosynthetic eukaryotes is essential in furthering our understanding of the impact of reversible protein acetylation on plant cell processes. Results We report a genome-scale analysis of lysine acetyltransferase (KAT)- and lysine deacetylase (KDAC)-families from 53 photosynthetic eukaryotes. KAT and KDAC orthologs were identified in sequenced genomes ranging from glaucophytes and algae to land plants and then analyzed for evolutionary relationships. Based on consensus molecular phylogenetic and subcellular localization data we found new sub-classes of enzymes in established KAT- and KDAC-families. Specifically, we identified a non-photosynthetic origin of the HD-tuin family KDACs, a new monocot-specific Class I HDA-family sub-class, and a phylogenetically distinct Class II algal/heterokont sub-class which maintains an ankyrin domain not conserved in land plant Class II KDACs. Protein structure analysis showed that HDA- and SRT-KDACs exist as bare catalytic subunits with highly conserved median protein length, while all KATs maintained auxiliary domains, with CBP- and TAFII250-KATs displaying protein domain gain and loss over the course of photosynthetic eukaryote evolution in addition to variable protein length. Lastly, promoter element enrichment analyses across species revealed conserved cis-regulatory sequences that support KAT and KDAC involvement in the regulation of plant development, cold/drought stress response, as well as cellular processes such as the circadian clock. Conclusions Our results reveal new evolutionary, structural, and biological insights into the KAT- and KDAC-families of photosynthetic eukaryotes, including evolutionary parallels to protein kinases and protein phosphatases. Further, we provide a comprehensive annotation framework through our extensive phylogenetic analysis, from which future research investigating aspects of protein acetylation in plants can use to position new findings in a broader context.
en_US
dc.language.iso
en
en_US
dc.publisher
BioMed Central
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Lysine Deacetylase
en_US
dc.subject
Post-translational modifications
en_US
dc.subject
Genomics
en_US
dc.subject
Lysine Acetyltransferase
en_US
dc.subject
Photosynthetic eukaryotes
en_US
dc.subject
Protein Acetylation
en_US
dc.title
Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
BMC Genomics
ethz.journal.volume
18
en_US
ethz.pages.start
514
en_US
ethz.size
20 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02541 - Institut für Molekulare Pflanzenbiologie / Institute of Molecular Plant Biology::03554 - Gruissem, Wilhelm / Gruissem, Wilhelm
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02541 - Institut für Molekulare Pflanzenbiologie / Institute of Molecular Plant Biology::03554 - Gruissem, Wilhelm / Gruissem, Wilhelm
ethz.date.deposited
2017-10-06T02:22:43Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-12-06T08:59:18Z
ethz.rosetta.lastUpdated
2018-11-06T05:00:19Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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