Zhou, H, Finkemeier, I, Guan, W et al. (11 more authors) (2018) Oxidative stress‐triggered interactions between the succinyl‐ and acetyl‐proteomes of rice leaves. Plant, Cell and Environment, 41 (5). pp. 1139-1153. ISSN 0140-7791
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 John Wiley & Sons Ltd. This is the peer reviewed version of the following article: Zhou H, Finkemeier I, Guan W, et al. Oxidative stress-triggered interactions between the succinyl- and acetyl-proteomes of rice leaves. Plant Cell Environ. 2018, which has been published in final form at https://doi.org/10.1111/pce.13100. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. |
Keywords: | catalase; glutathione S transferase; post-translational modifications; photosynthesis |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 Jan 2018 16:16 |
Last Modified: | 10 Nov 2018 01:39 |
Status: | Published |
Publisher: | Wiley-Blackwell |
Identification Number: | 10.1111/pce.13100 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:126055 |