The linker protein ApcI regulates light harvesting under red light in Synechocystis sp. PCC 6803

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652079%3A_____%2F25%3A00638013" target="_blank" >RIV/86652079:_____/25:00638013 - isvavai.cz</a>

Výsledek na webu

<a href="https://pubmed.ncbi.nlm.nih.gov/40479507/" target="_blank" >https://pubmed.ncbi.nlm.nih.gov/40479507/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/plcell/koaf144" target="_blank" >10.1093/plcell/koaf144</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The linker protein ApcI regulates light harvesting under red light in Synechocystis sp. PCC 6803

Popis výsledku v původním jazyce

Phycobilisomes (PBSs) are versatile cyanobacterial antenna complexes that harvest light energy to drive photosynthesis. They can adapt to various light conditions, for example, dismantling under high light to prevent photo-oxidation and arranging in rows under low light to increase light harvesting efficiency. Light quality also influences PBS structure and function, as observed nunder far-red light exposure. Here, we describe a PBS linker protein, ApcI (previously hypothetical protein Sll1911), expressed specifically under red light (620 nm) or upon chemically induced reduction of the plastoquinone pool. We characterized ApcI in Synechocystis sp. PCC 6803 using mutant analyses, PBS binding experiments, and protein interaction studies. Deletion of apcI nconferred high light tolerance on Synechocystis sp. PCC 6803 compared to the wild-type strain, leading to reduced energy transfer from PBSs to the photosystems under high light. Binding experiments revealed that ApcI replaces the linker protein ApcG at the nmembrane-facing side of the PBS core via a paralogous C-terminal motif. Additionally, the N-terminal region of ApcI interacts with photosystem II. Our findings highlight the importance of PBS remodeling for adaptation to different light conditions. The characterization of ApcI provides insight into the mechanisms by which cyanobacteria optimize light harvesting in response to nvarying light conditions.

Název v anglickém jazyce

The linker protein ApcI regulates light harvesting under red light in Synechocystis sp. PCC 6803

Popis výsledku anglicky

Phycobilisomes (PBSs) are versatile cyanobacterial antenna complexes that harvest light energy to drive photosynthesis. They can adapt to various light conditions, for example, dismantling under high light to prevent photo-oxidation and arranging in rows under low light to increase light harvesting efficiency. Light quality also influences PBS structure and function, as observed nunder far-red light exposure. Here, we describe a PBS linker protein, ApcI (previously hypothetical protein Sll1911), expressed specifically under red light (620 nm) or upon chemically induced reduction of the plastoquinone pool. We characterized ApcI in Synechocystis sp. PCC 6803 using mutant analyses, PBS binding experiments, and protein interaction studies. Deletion of apcI nconferred high light tolerance on Synechocystis sp. PCC 6803 compared to the wild-type strain, leading to reduced energy transfer from PBSs to the photosystems under high light. Binding experiments revealed that ApcI replaces the linker protein ApcG at the nmembrane-facing side of the PBS core via a paralogous C-terminal motif. Additionally, the N-terminal region of ApcI interacts with photosystem II. Our findings highlight the importance of PBS remodeling for adaptation to different light conditions. The characterization of ApcI provides insight into the mechanisms by which cyanobacteria optimize light harvesting in response to nvarying light conditions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Cell

ISSN

1040-4651

e-ISSN

1532-298X

Svazek periodika

37

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

15

Strana od-do

koaf144

Kód UT WoS článku

001539529400001

EID výsledku v databázi Scopus

2-s2.0-105011769123