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Antenna Protein Clustering In Vitro Unveiled by Fluorescence Correlation Spectroscopy
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SYSNO ASEP 0542531 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Antenna Protein Clustering In Vitro Unveiled by Fluorescence Correlation Spectroscopy Author(s) Crepin, Aurelia (MBU-M) ORCID
Cunill-Semanat, Edel (MBU-M)
Kuthanová Trsková, Eliška (MBU-M) ORCID
Belgio, Erica (MBU-M)
Kaňa, Radek (MBU-M) RID, ORCIDArticle number 2969 Source Title International Journal of Molecular Sciences. - : MDPI
Roč. 22, č. 6 (2021)Number of pages 18 s. Language eng - English Country CH - Switzerland Keywords photosynthesis ; photoprotection ; antenna proteins ; non-photochemical quenching ; fluorescence correlation spectroscopy ; detergent critical micelle concentration ; protein oligomerization Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GJ17-02363Y GA ČR - Czech Science Foundation (CSF) GA19-11494S GA ČR - Czech Science Foundation (CSF) ED2.1.00/19.0392 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000645718900001 EID SCOPUS 85102435363 DOI 10.3390/ijms22062969 Annotation Antenna protein aggregation is one of the principal mechanisms considered effective in protecting phototrophs against high light damage. Commonly, it is induced, in vitro, by decreasing detergent concentration and pH of a solution of purified antennas, the resulting reduction in fluorescence emission is considered to be representative of non-photochemical quenching in vivo. However, little is known about the actual size and organization of antenna particles formed by this means, and hence the physiological relevance of this experimental approach is questionable. Here, a quasi-single molecule method, fluorescence correlation spectroscopy (FCS), was applied during in vitro quenching of LHCII trimers from higher plants for a parallel estimation of particle size, fluorescence, and antenna cluster homogeneity in a single measurement. FCS revealed that, below detergent critical micelle concentration, low pH promoted the formation of large protein oligomers of sizes up to micrometers, and therefore is apparently incompatible with thylakoid membranes. In contrast, LHCII clusters formed at high pH were smaller and homogenous, and yet still capable of efficient quenching. The results altogether set the physiological validity limits of in vitro quenching experiments. Our data also support the idea that the small, moderately quenching LHCII oligomers found at high pH could be relevant with respect to non-photochemical quenching in vivo. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2022 Electronic address https://www.mdpi.com/1422-0067/22/6/2969
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