dc.identifier.uri |
http://dx.doi.org/10.15488/11684 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/11777 |
|
dc.contributor.author |
König, Ann-Christine
|
eng |
dc.contributor.author |
Hartl, Markus
|
eng |
dc.contributor.author |
Pham, Phuong Anh
|
eng |
dc.contributor.author |
Laxa, Miriam
|
eng |
dc.contributor.author |
Boersema, Paul J.
|
eng |
dc.contributor.author |
Orwat, Anne
|
eng |
dc.contributor.author |
Kalitventseva, Ievgeniia
|
eng |
dc.contributor.author |
Plöchinger, Magdalena
|
eng |
dc.contributor.author |
Braun, Hans-Peter
|
eng |
dc.contributor.author |
Leister, Dario
|
eng |
dc.contributor.author |
Mann, Matthias
|
eng |
dc.contributor.author |
Wachter, Andreas
|
eng |
dc.contributor.author |
Fernie, Alisdair R.
|
eng |
dc.contributor.author |
Finkemeier, Iris
|
eng |
dc.date.accessioned |
2022-01-13T14:37:48Z |
|
dc.date.available |
2022-01-13T14:37:48Z |
|
dc.date.issued |
2014 |
eng |
dc.identifier.citation |
König, A.-C.; Hartl, M.; Pham, P.A.; Laxa, M.; Boersema, P.J. et alI.: The Arabidopsis class II sirtuin is a lysine deacetylase and interacts with mitochondrial energy metabolism. In: Plant Physiology 164 (2014), Nr. 3, S. 1401-1414. DOI: https://doi.org/10.1104/pp.113.232496 |
eng |
dc.description.abstract |
The posttranslational regulation of proteins by lysine (Lys) acetylation has recently emerged to occur not only on histones, but also on organellar proteins in plants and animals. In particular, the catalytic activities of metabolic enzymes have been shown to be regulated by Lys acetylation. The Arabidopsis (Arabidopsis thaliana) genome encodes two predicted sirtuin-type Lys deacetylases, of which only Silent Information Regulator2 homolog (SRT2) contains a predicted presequence for mitochondrial targeting. Here, we have investigated the function of SRT2 in Arabidopsis. We demonstrate that SRT2 functions as a Lys deacetylase in vitro and in vivo. We show that SRT2 resides predominantly at the inner mitochondrial membrane and interacts with a small number of protein complexes mainly involved in energy metabolism and metabolite transport. Several of these protein complexes, such as the ATP synthase and the ATP/ADP carriers, show an increase in Lys acetylation in srt2 loss-of-function mutants. The srt2 plants display no growth phenotype but rather a metabolic phenotype with altered levels in sugars, amino acids, and ADP contents. Furthermore, coupling of respiration to ATP synthesis is decreased in these lines, while the ADP uptake into mitochondria is significantly increased. Our results indicate that SRT2 is important in fine-tuning mitochondrial energy metabolism. |
eng |
dc.language.iso |
eng |
eng |
dc.publisher |
Rockville, Md. : American Society of Plant Physiologists |
eng |
dc.relation.ispartofseries |
Plant Physiology 164 (2014), Nr. 3 |
eng |
dc.rights |
CC BY 4.0 Unported |
eng |
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
eng |
dc.subject |
adenosine diphosphate |
eng |
dc.subject |
adenosine triphosphate |
eng |
dc.subject |
Arabidopsis protein |
eng |
dc.subject |
carbon |
eng |
dc.subject |
histone deacetylase |
eng |
dc.subject |
lysine |
eng |
dc.subject |
messenger RNA |
eng |
dc.subject |
mitochondrial protein |
eng |
dc.subject |
nicotinamide adenine dinucleotide |
eng |
dc.subject |
sirtuin |
eng |
dc.subject |
SRT2 protein, Arabidopsis |
eng |
dc.subject |
acetylation |
eng |
dc.subject |
amino acid sequence |
eng |
dc.subject |
Arabidopsis |
eng |
dc.subject |
article |
eng |
dc.subject |
cell respiration |
eng |
dc.subject |
chemistry |
eng |
dc.subject |
energy metabolism |
eng |
dc.subject |
enzyme specificity |
eng |
dc.subject |
enzymology |
eng |
dc.subject |
gene inactivation |
eng |
dc.subject |
genetics |
eng |
dc.subject |
metabolism |
eng |
dc.subject |
mitochondrial membrane |
eng |
dc.subject |
mitochondrion |
eng |
dc.subject |
molecular genetics |
eng |
dc.subject |
nonsense mediated mRNA decay |
eng |
dc.subject |
phenotype |
eng |
dc.subject |
protein binding |
eng |
dc.subject |
protein transport |
eng |
dc.subject |
RNA splicing |
eng |
dc.subject |
Acetylation |
eng |
dc.subject |
Adenosine Diphosphate |
eng |
dc.subject |
Adenosine Triphosphate |
eng |
dc.subject |
Amino Acid Sequence |
eng |
dc.subject |
Arabidopsis |
eng |
dc.subject |
Arabidopsis Proteins |
eng |
dc.subject |
Carbon Isotopes |
eng |
dc.subject |
Cell Respiration |
eng |
dc.subject |
Energy Metabolism |
eng |
dc.subject |
Gene Knockout Techniques |
eng |
dc.subject |
Histone Deacetylases |
eng |
dc.subject |
Lysine |
eng |
dc.subject |
Mitochondria |
eng |
dc.subject |
Mitochondrial Membranes |
eng |
dc.subject |
Mitochondrial Proteins |
eng |
dc.subject |
Molecular Sequence Data |
eng |
dc.subject |
NAD |
eng |
dc.subject |
Nonsense Mediated mRNA Decay |
eng |
dc.subject |
Phenotype |
eng |
dc.subject |
Protein Binding |
eng |
dc.subject |
Protein Transport |
eng |
dc.subject |
RNA Splicing |
eng |
dc.subject |
RNA, Messenger |
eng |
dc.subject |
Sirtuins |
eng |
dc.subject |
Substrate Specificity |
eng |
dc.subject.ddc |
580 | Pflanzen (Botanik)
|
eng |
dc.title |
The Arabidopsis class II sirtuin is a lysine deacetylase and interacts with mitochondrial energy metabolism |
eng |
dc.type |
Article |
eng |
dc.type |
Text |
eng |
dc.relation.essn |
1532-2548 |
eng |
dc.relation.issn |
0032-0889 |
eng |
dc.relation.doi |
https://doi.org/10.1104/pp.113.232496 |
eng |
dc.bibliographicCitation.issue |
3 |
|
dc.bibliographicCitation.volume |
164 |
|
dc.bibliographicCitation.firstPage |
1401 |
|
dc.bibliographicCitation.lastPage |
1414 |
|
dc.description.version |
publishedVersion |
eng |
tib.accessRights |
frei zug�nglich |
eng |