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Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane
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SYSNO ASEP 0542412 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane Author(s) Kaňa, Radek (MBU-M) RID, ORCID
Steinbach, G. (HU)
Sobotka, Roman (MBU-M) RID, ORCID
Vamosi, G. (HU)
Komenda, Josef (MBU-M) RID, ORCIDArticle number 15 Source Title Life. - : MDPI
Roč. 11, č. 1 (2021)Number of pages 12 s. Language eng - English Country CH - Switzerland Keywords proteins mobility ; photosynthesis ; fcs ; thylakoids ; cyanobacteria Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects 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 000610396900001 EID SCOPUS 85098891459 DOI 10.3390/life11010015 Annotation Biological membranes were originally described as a fluid mosaic with uniform distribution of proteins and lipids. Later, heterogeneous membrane areas were found in many membrane systems including cyanobacterial thylakoids. In fact, cyanobacterial pigment-protein complexes (photosystems, phycobilisomes) form a heterogeneous mosaic of thylakoid membrane microdomains (MDs) restricting protein mobility. The trafficking of membrane proteins is one of the key factors for long-term survival under stress conditions, for instance during exposure to photoinhibitory light conditions. However, the mobility of unbound 'free' proteins in thylakoid membrane is poorly characterized. In this work, we assessed the maximal diffusional ability of a small, unbound thylakoid membrane protein by semi-single molecule FCS (fluorescence correlation spectroscopy) method in the cyanobacterium Synechocystis sp. PCC6803. We utilized a GFP-tagged variant of the cytochrome b(6)f subunit PetC1 (PetC1-GFP), which was not assembled in the b(6)f complex due to the presence of the tag. Subsequent FCS measurements have identified a very fast diffusion of the PetC1-GFP protein in the thylakoid membrane (D = 0.14 2.95 mu m(2)s(-1)). This means that the mobility of PetC1-GFP was comparable with that of free lipids and was 50-500 times higher in comparison to the mobility of proteins (e.g., IsiA, LHCII-light-harvesting complexes of PSII) naturally associated with larger thylakoid membrane complexes like photosystems. Our results thus demonstrate the ability of free thylakoid-membrane proteins to move very fast, revealing the crucial role of protein-protein interactions in the mobility restrictions for large thylakoid protein complexes. 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/2075-1729/11/1/15
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