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Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897491" target="_blank" >RIV/60076658:12310/18:43897491 - isvavai.cz</a>

  • Result on the web

    <a href="https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/1873-3468.13222" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/1873-3468.13222</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/1873-3468.13222" target="_blank" >10.1002/1873-3468.13222</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase

  • Original language description

    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/Oxal 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 syntheses in a cyanobacterial host. Synthesis of algal and plant chlorophyll syntheses 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    FEBS Letters

  • ISSN

    0014-5793

  • e-ISSN

  • Volume of the periodical

    592

  • Issue of the periodical within the volume

    18

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    3062-3073

  • UT code for WoS article

    000445330800005

  • EID of the result in the Scopus database

    2-s2.0-85053276252