<i>Paracoccus</i> as a Free‐Living Mitochondrion

John, P. S.

doi:10.1111/j.1749-6632.1987.tb40604.x

Cited by 9 publications

(5 citation statements)

References 58 publications

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“…The presence of an a purple bacteria (R. rubrum) at the base of this lineage (Fig. 5) confirms the results obtained on the basis ofrRNA, cytochrome c, and other evidence (Stewart and Mattox 1984;Yang et al 1985;John 1987;Cedergren et al 1988 Fig. 6.…”

Section: The Mitochondrial/nuclear Lineagesupporting

confidence: 82%

ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies

et al. 1992

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The 38 sequences of the ATPase c/III/9 gene determined in bacteria, fungi, mammals, and higher plants have been used to construct phylogenetic trees by distance matrix and parsimony methods (checked by bootstrapping); alignments have been performed on the deduced amino-acid sequences and then transferred back to the nucleotide sequences. Three lineages stand out: (1) eubacteria (except cyanobacteria and alpha purple bacteria), (2) chloroplasts, together with cyanobacteria, and (3) mitochondria together with nuclei and alpha purple bacteria. The clear monophyly of the mitochondrial/nuclear lineage, taken all together, strongly suggests that the nuclear copies of the gene now residing in the eukaryotic nucleus originate from a mitochondrial transfer. Within this lineage, metaphytes emerge late and as a cohesive group, after fungi (as a dispersed group) and metazoa, yielding an order that markedly differs from that obtained through typical RNA nuclear molecules. The possible biphyletic origin of mitochondria based on mitochondrial rRNA sequences is not evidenced by these sequences. Internal branches within both the chloroplastic and the mitochondrial lineages are consistent with botanical evolutionary schemes based on morphological characters. In spite of its relatively small size, the ATPase c/III/9 gene therefore displays remarkable properties as a phylogenetic index and adds a new tool for molecular evolutionary reconstructions, especially within the metaphytes.

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Section: The Mitochondrial/nuclear Lineagesupporting

confidence: 82%

ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies

et al. 1992

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“…It is generally accepted that the F 1 F O -ATPase of the α-proteobacteria is a direct predecessor of the mitochondrial enzyme because the pre-endosymbiont that evolved into the actual mitochondria most likely came from an ancestral α-proteobacteria, in concordance with the endosymbiotic theory promoted by Lynn Margulis [ 12 ] and more recent genomic analyses [ 75 , 76 ]. Several years ago, Paracoccus denitrificans was considered closely related to the free-living ancestor of the actual mitochondria [ 77 , 78 , 79 , 80 ], and it was even considered a microorganism similar to a free-living mitochondrion [ 81 ]. However, more recently, it is well accepted that other α-proteobacteria, such as those in the Rickettsiales order, might be phylogenetically closer to the actual mitochondria [ 82 ].…”

Section: Resultsmentioning

confidence: 99%

Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IF1 Subunits of the F1FO-ATPase as Related to the Endosymbiotic Origin of Mitochondria

et al. 2022

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The F1FO-ATP synthase nanomotor synthesizes >90% of the cellular ATP of almost all living beings by rotating in the “forward” direction, but it can also consume the same ATP pools by rotating in “reverse.” To prevent futile F1FO-ATPase activity, several different inhibitory proteins or domains in bacteria (ε and ζ subunits), mitochondria (IF1), and chloroplasts (ε and γ disulfide) emerged to block the F1FO-ATPase activity selectively. In this study, we analyze how these F1FO-ATPase inhibitory proteins have evolved. The phylogeny of the α-proteobacterial ε showed that it diverged in its C-terminal side, thus losing both the inhibitory function and the ATP-binding/sensor motif that controls this inhibition. The losses of inhibitory function and the ATP-binding site correlate with an evolutionary divergence of non-inhibitory α-proteobacterial ε and mitochondrial δ subunits from inhibitory bacterial and chloroplastidic ε subunits. Here, we confirm the lack of inhibitory function of wild-type and C-terminal truncated ε subunits of P. denitrificans. Taken together, the data show that ζ evolved to replace ε as the primary inhibitor of the F1FO-ATPase of free-living α-proteobacteria. However, the ζ inhibitory function was also partially lost in some symbiotic α-proteobacteria and totally lost in some strictly parasitic α-proteobacteria such as the Rickettsiales order. Finally, we found that ζ and IF1 likely evolved independently via convergent evolution before and after the endosymbiotic origin mitochondria, respectively. This led us to propose the ε and ζ subunits as tracer genes of the pre-endosymbiont that evolved into the actual mitochondria.

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“…Physiologically Paracoccus is a remarkably versatile bacterium. Under aerobic conditions the membrane-bound electron-transport chain closely resembles that of today's mitochondria [14]. All classical complexes of mitochondrial electrontransport have been isolated from this bacterium [15][16][17][18], the best characterized being complex III and IV.…”

Section: Introductionmentioning

confidence: 99%

Genetics of Paracoccus denitrificans

Steinrücke

Ludwig

1993

FEMS Microbiology Letters

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Paracoccus has approx. 15 subunits [28]. The transcriptional organization of this NDH-l-cluster is presently unknown. NQ01 and NQ02 code for flavoproteins, NQ03 to NQ06 are genes for iron-sulfur proteins whereas NQ07 to NQ014 code for polypeptides of the hydrophobic protein fraction [28]. The gene order in this cluster is NQ07, NQ06, NQ05, NQ04, NO02, NQ01 NQ03, NQ08 NQ09, NQ010, NQ011, NQO12, NQ013, and NQ014.Upstream of NQ07 an open reading frame with homology to Escherichia coli uvrA is found. A reading frame with homology to E. coli biotin acetyl-CoA carboxylase ligase has been found downstream of the cluster [28].Sequences for two genes, NQ01 [29], encoding the NADH-binding subunit, and NQ02 [30], which codes for an iron-sulfur protein, have been published. Two URFs have been found; sequence similarities of URF2 to ctaG of the Paracoccus cta-operon suggest a possible role as an assembly protein, most probably in the attachment of iron [29,30,55]. Because of its simpler structure the Paracoccus complex is likely to play an important part in investigating inhibitory agents or the mode of complex formation during assembly. Mutant strains are presently not available.

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Paracoccus as a Free‐Living Mitochondrion

Cited by 9 publications

References 58 publications

ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies

ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies

Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IF1 Subunits of the F1FO-ATPase as Related to the Endosymbiotic Origin of Mitochondria

Genetics of Paracoccus denitrificans

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