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Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane
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SYSNO ASEP 0542412 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane Tvůrce(i) Kaňa, Radek (MBU-M) RID, ORCID
Steinbach, G. (HU)
Sobotka, Roman (MBU-M) RID, ORCID
Vamosi, G. (HU)
Komenda, Josef (MBU-M) RID, ORCIDČíslo článku 15 Zdroj.dok. Life. - : MDPI
Roč. 11, č. 1 (2021)Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova proteins mobility ; photosynthesis ; fcs ; thylakoids ; cyanobacteria Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GA19-11494S GA ČR - Grantová agentura ČR ED2.1.00/19.0392 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 000610396900001 EID SCOPUS 85098891459 DOI 10.3390/life11010015 Anotace 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2022 Elektronická adresa https://www.mdpi.com/2075-1729/11/1/15
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