The high-light-induced protein SliP4 binds to NDH1 and photosystems facilitating cyclic electron transport and state transition in Synechocystis sp. PCC 6803

© 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation.

Détails bibliographiques
Publié dans:The New phytologist. - 1979. - 239(2023), 3 vom: 06. Aug., Seite 1083-1097
Auteur principal: Alvarenga-Lucius, Luna (Auteur)
Autres auteurs: Linhartová, Markéta, Schubert, Hendrik, Maaß, Sandra, Becher, Dörte, Hess, Wolfgang R, Sobotka, Roman, Hagemann, Martin
Format: Article en ligne
Langue:English
Publié: 2023
Accès à la collection:The New phytologist
Sujets:Journal Article Research Support, Non-U.S. Gov't NDH1 acclimation fluorescence high light photosynthesis superoxide dismutase thylakoid Photosynthetic Reaction Center Complex Proteins plus... Bacterial Proteins Photosystem II Protein Complex Photosystem I Protein Complex
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520 |a An increasing number of small proteins has been identified in the genomes of well-annotated organisms, including the model cyanobacterium Synechocystis sp. PCC 6803. We describe a newly assigned protein comprising 37 amino acids that is encoded upstream of the superoxide dismutase SodB encoding gene. To clarify the role of SliP4, we analyzed a Synechocystis sliP4 mutant and a strain containing a fully active, Flag-tagged variant of SliP4 (SliP4.f). The initial hypothesis that this small protein might be functionally related to SodB could not be supported. Instead, we provide evidence that it fulfills important functions related to the organization of photosynthetic complexes. Therefore, we named it a small light-induced protein of 4 kDa, SliP4. This protein is strongly induced under high-light conditions. The lack of SliP4 causes a light-sensitive phenotype due to impaired cyclic electron flow and state transitions. Interestingly, SliP4.f was co-isolated with NDH1 complex and both photosystems. The interaction between SliP4.f and all three types of complexes was further confirmed by additional pulldowns and 2D-electrophoreses. We propose that the dimeric SliP4 serves as a molecular glue promoting the aggregation of thylakoid complexes, which contributes to different electron transfer modes and energy dissipation under stress conditions 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a NDH1 
650 4 |a acclimation 
650 4 |a fluorescence 
650 4 |a high light 
650 4 |a photosynthesis 
650 4 |a superoxide dismutase 
650 4 |a thylakoid 
650 7 |a Photosynthetic Reaction Center Complex Proteins  |2 NLM 
650 7 |a Bacterial Proteins  |2 NLM 
650 7 |a Photosystem II Protein Complex  |2 NLM 
650 7 |a Photosystem I Protein Complex  |2 NLM 
700 1 |a Linhartová, Markéta  |e verfasserin  |4 aut 
700 1 |a Schubert, Hendrik  |e verfasserin  |4 aut 
700 1 |a Maaß, Sandra  |e verfasserin  |4 aut 
700 1 |a Becher, Dörte  |e verfasserin  |4 aut 
700 1 |a Hess, Wolfgang R  |e verfasserin  |4 aut 
700 1 |a Sobotka, Roman  |e verfasserin  |4 aut 
700 1 |a Hagemann, Martin  |e verfasserin  |4 aut 
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