An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms

David Rauh, Frank Fischer, Melanie Gertz, Mahadevan Lakshminarasimhan, Tim Bergbrede, Firouzeh Aladini, Christian Kambach, Christian F. W. Becker, Johannes Zerweck, Mike Schutkowski and Clemens Steegborn ()
Additional contact information
David Rauh: Institute for Biochemistry and Biotechnology, Martin Luther University
Frank Fischer: University of Bayreuth, Universitätsstraße 30
Melanie Gertz: University of Bayreuth, Universitätsstraße 30
Mahadevan Lakshminarasimhan: University of Bayreuth, Universitätsstraße 30
Tim Bergbrede: Lead Discovery Center GmbH, Otto-Hahn-Straße 15
Firouzeh Aladini: Technical University Munich, Lichtenbergstraße 4
Christian Kambach: University of Bayreuth, Universitätsstraße 30
Christian F. W. Becker: Technical University Munich, Lichtenbergstraße 4
Johannes Zerweck: JPT Peptide Technologies GmbH, Volmerstraße 5
Mike Schutkowski: Institute for Biochemistry and Biotechnology, Martin Luther University
Clemens Steegborn: University of Bayreuth, Universitätsstraße 30

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract Sirtuin enzymes regulate metabolism and aging processes through deacetylation of acetyl-lysines in target proteins. More than 6,800 mammalian acetylation sites are known, but few targets have been assigned to most sirtuin isoforms, hampering our understanding of sirtuin function. Here we describe a peptide microarray system displaying 6,802 human acetylation sites for the parallel characterisation of their modification by deacetylases. Deacetylation data for all seven human sirtuins obtained with this system reveal isoform-specific substrate preferences and deacetylation substrate candidates for all sirtuin isoforms, including Sirt4. We confirm malate dehydrogenase protein as a Sirt3 substrate and show that peroxiredoxin 1 and high-mobility group B1 protein are deacetylated by Sirt5 and Sirt1, respectively, at the identified sites, rendering them likely new in vivo substrates. Our microarray platform enables parallel studies on physiological acetylation sites and the deacetylation data presented provide an exciting resource for the identification of novel substrates for all human sirtuins.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms3327 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3327

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms3327

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().