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

Titelangaben

Rauh, David ; Fischer, Frank ; Gertz, Melanie ; Lakshminarasimhan, Mahadevan ; Bergbrede, Tim ; Aladini, Firouzeh ; Kambach, Christian ; Becker, Christian F. W. ; Zerweck, Johannes ; Schutkowski, Mike ; Steegborn, Clemens:
An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms.
In: Nature Communications. Bd. 4 (2013) . - S. 2327.
ISSN 2041-1723
DOI: https://doi.org/10.1038/ncomms3327

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.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Zusätzliche Informationen: PubMed-ID: 23995836
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie > Lehrstuhl Biochemie I - Proteinbiochemie der Signaltransduktion - Univ.-Prof. Dr. Clemens Steegborn
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
Eingestellt am: 20 Apr 2015 12:50
Letzte Änderung: 20 Apr 2015 12:50
URI: https://eref.uni-bayreuth.de/id/eprint/10424