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A mitochondrion-free eukaryote contains proteins capable of import into an exogenous mitochondrion-related organelle

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00567556" target="_blank" >RIV/61388963:_____/23:00567556 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/23:10456791

  • Result on the web

    <a href="https://doi.org/10.1098/rsob.220238" target="_blank" >https://doi.org/10.1098/rsob.220238</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1098/rsob.220238" target="_blank" >10.1098/rsob.220238</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A mitochondrion-free eukaryote contains proteins capable of import into an exogenous mitochondrion-related organelle

  • Original language description

    The endobiotic flagellate Monocercomonoides exilis is the only known eukaryote to have lost mitochondria and all its associated proteins in its evolutionary past. This final stage of the mitochondrial evolutionary pathway may serve as a model to explain events at their very beginning such as the initiation of protein import. We have assessed the capability of proteins from this eukaryote to enter emerging mitochondria using a specifically designed in vitro assay. Hydrogenosomes (reduced mitochondria) of Trichomonas vaginalis were incubated with a soluble protein pool derived from a cytosolic fraction of M. exilis, and proteins entering hydrogenosomes were subsequently detected by mass spectrometry. The assay detected 19 specifically and reproducibly imported proteins, and in 14 cases the import was confirmed by the overexpression of their tagged version in T. vaginalis. In most cases, only a small portion of the signal reached the hydrogenosomes, suggesting specific but inefficient transport. Most of these proteins represent enzymes of carbon metabolism, and none exhibited clear signatures of proteins targeted to hydrogenosomes or mitochondria, which is consistent with their inefficient import. The observed phenomenon may resemble a primaeval type of protein import which might play a role in the establishment of the organelle and shaping of its proteome in the initial stages of endosymbiosis.

  • 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

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Open Biology

  • ISSN

    2046-2441

  • e-ISSN

    2046-2441

  • Volume of the periodical

    13

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    220238

  • UT code for WoS article

    000912067900005

  • EID of the result in the Scopus database

    2-s2.0-85146101955