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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F11%3A10105549%21RIV12-MSM-11310___
rdf:type
skos:Concept n11:Vysledek
rdfs:seeAlso
http://mbe.oxfordjournals.org/content/early/2011/02/03/molbev.msr032.full.pdf+html
dcterms:description
Most of the major groups of eukaryotes have microbial representatives that thrive in low oxygen conditions. Those that have been studied in detail generate ATP via pathways involving anaerobically functioning enzymes of pyruvate catabolism that are typically absent in aerobic eukaryotes and whose origins remain controversial. Pyruvate formate lyase (Pfl) catalyzes the non-oxidative generation of formate and acetyl-Coenzyme A (CoA) from pyruvate and CoA and is activated by Pfl activating enzyme (Pfla). To clarify the origins of this pathway, we have comprehensively searched for homologs of Pfl and Pfla in publicly available large-scale eukaryotic genomic and cDNA sequencing data, including our own from the anaerobic amoebozoan Mastigamoeba balamuthi. Surprisingly, we find that these enzymes are widely distributed, and are present in diverse facultative or obligate anaerobic eukaryotic representatives of the archaeplastidan, metazoan, amoebozoan, and haptophyte lineages. Using maximum likelihood and Bayesian phylogenetic methods we show that the eukaryotic Pfl and Pfla sequences each form monophyletic groups that are most closely related to homologs in firmicute gram-positive bacteria. Topology tests exclude both α-proteobacterial and cyanobacterial affinities for these genes suggesting that neither originated from the endosymbiotic ancestors of mitochondria or chloroplasts. Furthermore, the topologies of the eukaryote portion of the Pfl and Pfla trees significantly differ from well-accepted eukaryote relationships. Collectively, these results indicate that the Pfl pathway was first acquired by lateral gene transfer into a eukaryotic lineage most probably from a firmicute bacterial lineage, and that it has since been spread across diverse eukaryotic groups by more recent eukaryote-to-eukaryote transfer events. Most of the major groups of eukaryotes have microbial representatives that thrive in low oxygen conditions. Those that have been studied in detail generate ATP via pathways involving anaerobically functioning enzymes of pyruvate catabolism that are typically absent in aerobic eukaryotes and whose origins remain controversial. Pyruvate formate lyase (Pfl) catalyzes the non-oxidative generation of formate and acetyl-Coenzyme A (CoA) from pyruvate and CoA and is activated by Pfl activating enzyme (Pfla). To clarify the origins of this pathway, we have comprehensively searched for homologs of Pfl and Pfla in publicly available large-scale eukaryotic genomic and cDNA sequencing data, including our own from the anaerobic amoebozoan Mastigamoeba balamuthi. Surprisingly, we find that these enzymes are widely distributed, and are present in diverse facultative or obligate anaerobic eukaryotic representatives of the archaeplastidan, metazoan, amoebozoan, and haptophyte lineages. Using maximum likelihood and Bayesian phylogenetic methods we show that the eukaryotic Pfl and Pfla sequences each form monophyletic groups that are most closely related to homologs in firmicute gram-positive bacteria. Topology tests exclude both α-proteobacterial and cyanobacterial affinities for these genes suggesting that neither originated from the endosymbiotic ancestors of mitochondria or chloroplasts. Furthermore, the topologies of the eukaryote portion of the Pfl and Pfla trees significantly differ from well-accepted eukaryote relationships. Collectively, these results indicate that the Pfl pathway was first acquired by lateral gene transfer into a eukaryotic lineage most probably from a firmicute bacterial lineage, and that it has since been spread across diverse eukaryotic groups by more recent eukaryote-to-eukaryote transfer events.
dcterms:title
Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute
skos:prefLabel
Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute
skos:notation
RIV/00216208:11310/11:10105549!RIV12-MSM-11310___
n11:predkladatel
n12:orjk%3A11310
n4:aktivita
n19:Z
n4:aktivity
Z(MSM0021620828)
n4:cisloPeriodika
7
n4:dodaniDat
n9:2012
n4:domaciTvurceVysledku
n15:2819562
n4:druhVysledku
n14:J
n4:duvernostUdaju
n18:S
n4:entitaPredkladatele
n17:predkladatel
n4:idSjednocenehoVysledku
198139
n4:idVysledku
RIV/00216208:11310/11:10105549
n4:jazykVysledku
n8:eng
n4:klicovaSlova
firmicute; laterally; acquired; were; enzyme; activating; its; lyase; formate; pyruvate; Eukaryotic
n4:klicoveSlovo
n5:Eukaryotic n5:laterally n5:activating n5:formate n5:acquired n5:its n5:pyruvate n5:were n5:lyase n5:enzyme n5:firmicute
n4:kodStatuVydavatele
US - Spojené státy americké
n4:kontrolniKodProRIV
[C72C15702167]
n4:nazevZdroje
Molecular Biology and Evolution
n4:obor
n21:EB
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
3
n4:rokUplatneniVysledku
n9:2011
n4:svazekPeriodika
28
n4:tvurceVysledku
Stairs, Courtney Hampl, Vladimír Roger, Andrew
n4:wos
000291756400013
n4:zamer
n16:MSM0021620828
s:issn
0737-4038
s:numberOfPages
13
n20:doi
10.1093/molbev/msr032
n10:organizacniJednotka
11310