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Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase.
Proctor, Matthew S; Chidgey, Jack W; Shukla, Mahendra K; Jackson, Philip J; Sobotka, Roman; Hunter, C Neil; Hitchcock, Andrew.
Afiliação
  • Proctor MS; Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
  • Chidgey JW; Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
  • Shukla MK; Institute of Microbiology, Czech Academy of Sciences, Center Algatech, Trebon, Czech Republic.
  • Jackson PJ; Faculty of Science, University of South Bohemia, Ceské Budejovice, Czech Republic.
  • Sobotka R; Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
  • Hunter CN; Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, UK.
  • Hitchcock A; Institute of Microbiology, Czech Academy of Sciences, Center Algatech, Trebon, Czech Republic.
FEBS Lett ; 592(18): 3062-3073, 2018 09.
Article em En | MEDLINE | ID: mdl-30107031
ABSTRACT
In the model cyanobacterium Synechocystis sp. PCC 6803, the terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), forms a complex with high light-inducible proteins, the photosystem II assembly factor Ycf39 and the YidC/Alb3/OxaI membrane insertase, co-ordinating chlorophyll delivery with cotranslational insertion of nascent photosystem polypeptides into the membrane. To gain insight into the ubiquity of this assembly complex in higher photosynthetic organisms, we produced functional foreign chlorophyll synthases in a cyanobacterial host. Synthesis of algal and plant chlorophyll synthases allowed deletion of the otherwise essential native cyanobacterial gene. Analysis of purified protein complexes shows that the interaction with YidC is maintained for both eukaryotic enzymes, indicating that a ChlG-YidC/Alb3 complex may be evolutionarily conserved in algae and plants.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Carbono-Oxigênio Ligases / Proteínas de Arabidopsis / Complexo de Proteína do Fotossistema II / Synechocystis Tipo de estudo: Prognostic_studies Idioma: En Revista: FEBS Lett Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Carbono-Oxigênio Ligases / Proteínas de Arabidopsis / Complexo de Proteína do Fotossistema II / Synechocystis Tipo de estudo: Prognostic_studies Idioma: En Revista: FEBS Lett Ano de publicação: 2018 Tipo de documento: Article