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Xanthophyll carotenoids stabilise the association of cyanobacterial chlorophyll synthase with the LHC-like protein HliD

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    SYSNO ASEP0535059
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleXanthophyll carotenoids stabilise the association of cyanobacterial chlorophyll synthase with the LHC-like protein HliD
    Author(s) Proctor, M. S. (GB)
    Pazderník, Marek (MBU-M)
    Jackson, P. J. (GB)
    Pilný, Jan (MBU-M) ORCID
    Martin, E. C. (GB)
    Dickman, M. J. (GB)
    Canniffe, D. P. (GB)
    Johnson, M. P. (GB)
    Hunter, C. N. (GB)
    Sobotka, Roman (MBU-M) RID, ORCID
    Hitchcock, A. (GB)
    Source TitleBiochemical Journal. - : Portland Press - ISSN 0264-6021
    Roč. 477, č. 20 (2020), s. 4021-4036
    Number of pages16 s.
    Languageeng - English
    CountryGB - United Kingdom
    Keywordslight-inducible polypeptides ; synechocystis sp pcc-6803 ; photosystem-ii ; beta-carotene ; biosynthetic-pathway ; bind chlorophyll ; zeaxanthin ; myxoxanthophyll
    Subject RIVCE - Biochemistry
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsGX19-29225X GA ČR - Czech Science Foundation (CSF)
    Method of publishingOpen access
    Institutional supportMBU-M - RVO:61388971
    UT WOS000588274400004
    EID SCOPUS85094983874
    DOI10.1042/BCJ20200561
    AnnotationChlorophyll synthase (ChlG) catalyses a terminal reaction in the chlorophyll biosynthesis pathway, attachment of phytol or geranylgeraniol to the C17 propionate of chlorophyllide. Cyanobacterial ChlG forms a stable complex with high light-inducible protein D (HliD), a small single-helix protein homologous to the third transmembrane helix of plant light-harvesting complexes (LHCs). The ChlG-HliD assembly binds chlorophyll, beta-carotene, zeaxanthin and myxoxanthophyll and associates with the YidC insertase, most likely to facilitate incorporation of chlorophyll into translated photosystem apoproteins. HliD independently coordinates chlorophyll and beta-carotene but the role of the xanthophylls, which appear to be exclusive to the core ChlG-HliD assembly, is unclear. Here we generated mutants of Synechocystis sp. PCC 6803 lacking specific combinations of carotenoids or HliD in a background with FLAG- or His-tagged ChlG. Immunoprecipitation experiments and analysis of isolated membranes demonstrate that the absence of zeaxanthin and myxoxanthophyll significantly weakens the interaction between HliD and ChlG. ChlG alone does not bind carotenoids and accumulation of the chlorophyllide substrate in the absence of xanthophylls indicates that activity/stability of the `naked' enzyme is perturbed. In contrast, the interaction of HliD with a second partner, the photosystem II assembly factor Ycf39, is preserved in the absence of xanthophylls. We propose that xanthophylls are required for the stable association of ChlG and HliD, acting as a ´molecular glue´ at the lateral transmembrane interface between these proteins, roles for zeaxanthin and myxoxanthophyll in ChlG-HliD complexation are discussed, as well as the possible presence of similar complexes between LHC-like proteins and chlorophyll biosynthesis enzymes in plants.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2021
    Electronic addresshttps://portlandpress.com/biochemj/article-abstract/477/20/4021/226545/Xanthophyll-carotenoids-stabilise-the-association?redirectedFrom=fulltext
Number of the records: 1  

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