Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/60077344:_____/21:00554417

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

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

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Biology - Basel

ISSN

2079-7737

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

10

Strana od-do

—

Kód UT WoS článku

000653409400001

EID výsledku v databázi Scopus

2-s2.0-85105803819