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The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration
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SYSNO ASEP 0508268 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration Author(s) Pazderník, Marek (MBU-M)
Mareš, Jan (MBU-M) ORCID
Pilný, Jan (MBU-M) ORCID
Sobotka, Roman (MBU-M) RID, ORCIDSource Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 294, č. 29 (2019), s. 11131-11143Number of pages 23 s. Language eng - English Country US - United States Keywords plant biochemistry ; photosynthetic pigment ; photosynthesis Subject RIV CE - Biochemistry OECD category Biochemistry and molecular biology R&D Projects LO1416 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA17-08755S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support MBU-M - RVO:61388971 UT WOS 000478717400007 EID SCOPUS 85069956143 DOI 10.1074/jbc.RA119.008434 Annotation Ferrochelatase (FeCh) is an essential enzyme catalyzing the synthesis of heme. Interestingly, in cyanobacteria, algae, and plants, FeCh possesses a conserved transmembrane chlorophyll a/b binding (CAB) domain that resembles the first and the third helix of light-harvesting complexes, including a chlorophyll-binding motif. Whether the FeCh CAB domain also binds chlorophyll is unknown. Here, using biochemical and radiolabeled precursor experiments, we found that partially inhibited activity of FeCh in the cyanobacterium Synechocystis PCC 6803 leads to overproduction of chlorophyll molecules that accumulate in the thylakoid membrane and, together with carotenoids, bind to FeCh. We observed that pigments bound to purified FeCh are organized in an energy-dissipative conformation and further show that FeCh can exist in vivo as a monomer or a dimer depending on its own activity. However, pigmented FeCh was purified exclusively as a dimer. Separately expressed and purified FeCH CAB domain contained a pigment composition similar to that of full-length FeCh and retained its quenching properties. Phylogenetic analysis suggested that the CAB domain was acquired by a fusion between FeCh and a single-helix, high light-inducible protein early in the evolution of cyanobacteria. Following this fusion, the FeCh CAB domain with a functional chlorophyll-binding motif was retained in all currently known cyanobacterial genomes except for a single lineage of endosymbiotic cyanobacteria. Our findings indicate that FeCh from Synechocystis exists mostly as a pigment-free monomer in cells but can dimerize, in which case its CAB domain creates a functional pigment-binding segment organized in an energy-dissipating configuration. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2020 Electronic address https://www.jbc.org/content/294/29/11131
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