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Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F12%3A00378838" target="_blank" >RIV/60077344:_____/12:00378838 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/12:43883515

  • Result on the web

    <a href="http://dx.doi.org/10.1073/pnas.1116067109" target="_blank" >http://dx.doi.org/10.1073/pnas.1116067109</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1073/pnas.1116067109" target="_blank" >10.1073/pnas.1116067109</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

  • Original language description

    Iron/sulfur cluster (ISC)-containing proteins are essential components of cells. In most eukaryotes, Fe/S clusters are synthesized by the mitochondrial ISC machinery, the cytosolic iron/sulfur assembly system, and, in photosynthetic species, a plastid sulfur-mobilization (SUF) system. Here we show that the anaerobic human protozoan parasite Blastocystis, in addition to possessing ISC and iron/sulfur assembly systems, expresses a fused version of the SufC and SufB proteins of prokaryotes that it has acquired by lateral transfer from an archaeon related to the Methanomicrobiales, an important lineage represented in the human gastrointestinal tract microbiome. Although components of the Blastocystis ISC system function within its anaerobic mitochondrion-related organelles and can functionally replace homologues in Trypanosoma brucei, its SufCB protein has similar biochemical properties to its prokaryotic homologues, functions within the parasite's cytosol, and is up-regulated under oxygen

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Proceedings of the National Academy of Sciences of the United States of America

  • ISSN

    0027-8424

  • e-ISSN

  • Volume of the periodical

    109

  • Issue of the periodical within the volume

    26

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    6

  • Pages from-to

    10426-10431

  • UT code for WoS article

    000306291400069

  • EID of the result in the Scopus database