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Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903491" target="_blank" >RIV/60076658:12310/21:43903491 - isvavai.cz</a>

  • Alternative codes found

    RIV/60077344:_____/21:00554417

  • Result on the web

    <a href="https://www.mdpi.com/2079-7737/10/5/386" target="_blank" >https://www.mdpi.com/2079-7737/10/5/386</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/biology10050386" target="_blank" >10.3390/biology10050386</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs

  • Original language description

    Simple Summary The heme pathway is essential for most of cellular life. In eukaryotic phototrophs, the entire pathway is plastid localized. Despite that, the enzyme responsible for the synthesis of hydroxymethylbilane, porphobilinogen deaminase, shows alpha-proteobacterial instead of expected cyanobacterial origins in rhodophytes, chlorophytes, plants, and most algae with complex plastid. However, no such enzyme has been found in the supposed partners of plastid endosymbioses, the heterotrophic eukaryotes, and cyanobacteria. I propose two scenarios explaining this phenomenon by either endosymbiotic gene transfer from the ancestor of mitochondria or a non-endosymbiotic lateral gene transfer from unspecified alpha-proteobacterium. Phylogenetic analysis of porphobilinogen deaminases does not reject any of the two proposed evolutionary scenarios. In most eukaryotic phototrophs, the entire heme synthesis is localized to the plastid, and enzymes of cyanobacterial origin dominate the pathway. Despite that, porphobilinogen deaminase (PBGD), the enzyme responsible for the synthesis of hydroxymethybilane in the plastid, shows phylogenetic affiliation to alpha-proteobacteria, the supposed ancestor of mitochondria. Surprisingly, no PBGD of such origin is found in the heme pathway of the supposed partners of the primary plastid endosymbiosis, a primarily heterotrophic eukaryote, and a cyanobacterium. It appears that alpha-proteobacterial PBGD is absent from glaucophytes but is present in rhodophytes, chlorophytes, plants, and most algae with complex plastids. This may suggest that in eukaryotic phototrophs, except for glaucophytes, either the gene from the mitochondrial ancestor was retained while the cyanobacterial and eukaryotic pseudoparalogs were lost in evolution, or the gene was acquired by non-endosymbiotic gene transfer from an unspecified alpha-proteobacterium and functionally replaced its cyanobacterial and eukaryotic counterparts.

  • 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

    10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology

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

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biology - Basel

  • ISSN

    2079-7737

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    10

  • Pages from-to

  • UT code for WoS article

    000653409400001

  • EID of the result in the Scopus database

    2-s2.0-85105803819