Zhou, H;
Finkemeier, I;
Guan, W;
Tossounian, M-A;
Wei, B;
Young, D;
Huang, J;
... Foyer, CH; + view all
(2018)
Oxidative stress‐triggered interactions between the succinyl‐ and acetyl‐proteomes of rice leaves.
Plant, Cell & Environment
, 41
(5)
pp. 1139-1153.
10.1111/pce.13100.
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Abstract
Protein lysine acylations, such as succinylation and acetylation, are important post‐translational modification (PTM) mechanisms, with key roles in cellular regulation. Antibody‐based affinity enrichment, high‐resolution liquid chromatography mass spectrometry analysis, and integrated bioinformatics analysis were used to characterize the lysine succinylome (Ksuc) and acetylome (Kace) of rice leaves. In total, 2,593 succinylated and 1,024 acetylated proteins were identified, of which 723 were simultaneously acetylated and succinylated. Proteins involved in photosynthetic carbon metabolism such as the large and small subunits of RuBisCO, ribosomal functions, and other key processes were subject to both PTMs. Preliminary insights into oxidant‐induced changes to the rice acetylome and succinylome were gained from treatments with hydrogen peroxide. Exposure to oxidative stress did not regulate global changes in the rice acetylome or succinylome but rather led to modifications on a specific subset of the identified sites. De‐succinylation of recombinant catalase (CATA) and glutathione S‐transferase (OsGSTU6) altered the activities of these enzymes showing that this PTM may have a regulatory function. These findings not only greatly extend the list of acetylated and/or succinylated proteins but they also demonstrate the close cooperation between these PTMs in leaf proteins with key metabolic functions.
| Type: | Article |
|---|---|
| Title: | Oxidative stress‐triggered interactions between the succinyl‐ and acetyl‐proteomes of rice leaves |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1111/pce.13100 |
| Publisher version: | https://doi.org/10.1111/pce.13100 |
| Language: | English |
| Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
| Keywords: | catalase, glutathione S transferase, post‐translational modifications, photosynthesis |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
| URI: | https://discovery-pp.ucl.ac.uk/id/eprint/10092591 |
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