Malondialdehyde enhances PsbP protein release during heat stress in Arabidopsis
Language English Country France Media print-electronic
Document type Journal Article
PubMed
37669610
DOI
10.1016/j.plaphy.2023.107984
PII: S0981-9428(23)00495-3
Knihovny.cz E-resources
- Keywords
- Heat stress, Lysine, Malondialdehyde, Photosystem II, Reactive oxygen species,
- MeSH
- Arabidopsis * MeSH
- Glutamic Acid MeSH
- Lysine MeSH
- Malondialdehyde MeSH
- Heat-Shock Response MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Glutamic Acid MeSH
- Lysine MeSH
- Malondialdehyde MeSH
Under environmental conditions, plants are exposed to various abiotic and biotic stress factors, which commonly cause the oxidation of lipids and proteins. Lipid peroxidation constantly produces malondialdehyde (MDA), a secondary product of lipid peroxidation, which is covalently bound to proteins forming MDA-protein adducts. The spatial distribution of MDA-protein adducts in Arabidopsis leaves shows that MDA-protein adducts are located in the chloroplasts, uniformly spread out over the thylakoid membrane. At the lumenal side of thylakoid membrane, MDA interacts with PsbP, an extrinsic subunit of the photosystem II (PSII), which is in electrostatic interaction with the PSII core proteins. Under heat stress, when MDA is moderately enhanced, the electrostatic interaction between PsbP and PSII core proteins is weakened, and PsbP with bound MDA is released in the lumen. It is proposed here that the electrophilic MDA is bound to the nucleophilic lysine residues of PsbP, which are involved in electrostatic interactions with the negatively charged glutamate of the PSII core protein. Our data provide crucial information about the MDA binding topology in the higher plant PSII complex, which is necessary to understand better the physiological functions of MDA for plant survival under stress.
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