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The C-terminal extension of ferrochelatase is critical for enzyme activity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F08%3A00315013" target="_blank" >RIV/61388971:_____/08:00315013 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12640/08:00009368

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    The C-terminal extension of ferrochelatase is critical for enzyme activity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803

  • Original language description

    We analysed the DH324 strain of Synechocystis sp. PCC 6803, which contains a truncated ferrochelatase enzyme lacking this C-terminal domain. Truncated FeCH was localized to the membrane fraction suggesting that the C-terminal domain is not necessary formembrane association of the enzyme. Measurements of enzyme activity and complementation experiments revealed that the DH324 mutation dramatically reduced activity of the FeCH. Moreover, the H324 mutant accumulated a large amount of protoporphyrin and levels of chlorophyll precursors were also significantly increased. Analysis of the recombinant full-length and truncated FeCHs demonstrated that the C-terminal extension is critical for activity of the FeCH and it is strictly required for oligomerization of this enzyme

  • Czech name

    C-terminální extenze enzymu ferochelatázy je nezbytná pro aktivitu enzymu a pro fungování biosyntetické dráhy tetrapyrolů u Synechocystis PCC6830

  • Czech description

    Analyzovali jsme kmen sinice Synechocystis sp. PCC 6803, obsahující zkrácenou formu enzymu ferochelatázy bez C-koncové domény. Zkráceny enzym byl lokalizován v membránové frakci, což ukazuje, že doména není nezbytná pro asociaci enzymu s membránou. Z měření aktivit a z komplementace vyplývalo, že mutace H324 dramaticky redukuje aktivitu ferochelatázy. Mimoto, mutant DH324 akumuloval velká množství protoporfyrinu and prekurzorů chlorofylu. Analýza rekombinantní úplné a zkrácené ferochelatatázy prokázala,že C-koncová doména je nezbytná pro aktivitu enzymu and pro jeho oligomerizaci

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2008

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Bacteriology

  • ISSN

    0021-9193

  • e-ISSN

  • Volume of the periodical

    190

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

  • UT code for WoS article

    000253825500027

  • EID of the result in the Scopus database