The TOM Complex of Amoebozoans: the Cases of the Amoeba Acanthamoeba castellanii and the Slime Mold Dictyostelium discoideum

Wojtkowska, Małgorzata; Buczek, Dorota; Stobienia, Olgierd; Karachitos, Andonis; Antoniewicz, Monika; Słocińska, Małgorzata; Makałowski, Wojciech; Kmita, Hanna

doi:10.1016/j.protis.2015.05.005

Cited by 17 publications

(11 citation statements)

References 65 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To settle the argument, determination of the Tom22 state in Amoebozoa is crucial because of its phylogenetic position. Genes annotated as Tom22 in the Amoebozoa TOM complex (Wojtkowska et al 2015; Buczek et al 2016) share no sequence similarity to known Tom22, as argued by Mani et al (2016). In contrast to the obscure Tom22, we found more reliable Tom22 orthologs in two sequenced Amoebozoa genomes ( D ictyostelium discoideum and Polysphondylium pallidum ): DDB0219756 and PPL_03846.…”

Section: Resultsmentioning

confidence: 61%

See 1 more Smart Citation

Origin and Evolutionary Alteration of the Mitochondrial Import System in Eukaryotic Lineages

Fukasawa

Oda

Tomii

et al. 2017

Molecular Biology and Evolution

View full text Add to dashboard Cite

Protein transport systems are fundamentally important for maintaining mitochondrial function. Nevertheless, mitochondrial protein translocases such as the kinetoplastid ATOM complex have recently been shown to vary in eukaryotic lineages. Various evolutionary hypotheses have been formulated to explain this diversity. To resolve any contradiction, estimating the primitive state and clarifying changes from that state are necessary. Here, we present more likely primitive models of mitochondrial translocases, specifically the translocase of the outer membrane (TOM) and translocase of the inner membrane (TIM) complexes, using scrutinized phylogenetic profiles. We then analyzed the translocases’ evolution in eukaryotic lineages. Based on those results, we propose a novel evolutionary scenario for diversification of the mitochondrial transport system. Our results indicate that presequence transport machinery was mostly established in the last eukaryotic common ancestor, and that primitive translocases already had a pathway for transporting presequence-containing proteins. Moreover, secondary changes including convergent and migrational gains of a presequence receptor in TOM and TIM complexes, respectively, likely resulted from constrained evolution. The nature of a targeting signal can constrain alteration to the protein transport complex.

show abstract

Section: Resultsmentioning

confidence: 61%

“…The most important alteration is the gain of a presequence receptor. It was reported recently that an Amoebozoa, Acanthamoeba castellanii TOM complex, has Tom20 and Tom22 (Wojtkowska et al 2015; Buczek et al 2016; Mani et al 2016). The orthology of the Amoebozoa Tom20 is important to ascertain the gain timing of Tom20.…”

Section: Resultsmentioning

confidence: 99%

Origin and Evolutionary Alteration of the Mitochondrial Import System in Eukaryotic Lineages

Fukasawa

Oda

Tomii

et al. 2017

Molecular Biology and Evolution

View full text Add to dashboard Cite

show abstract

“…Amoeba have traditionally been classified as protists and are now recognized as closely related to fungi and animals [ 53 , 60 ]. Consistently, Tom70 was identified in Acanthamoeba castellanii and Dicytostelium discoideum [ 61 , 62 ]. In contrast, Tom70 is virtually absent in the phylogenetically separate supergroup Excavata which includes Trichomonas vaginalis and Trypanosoma brucei [ 63 , 64 ].…”

Section: Evolution Of Tom70mentioning

confidence: 68%

The Mitochondrial Outer Membrane Protein Tom70-Mediator in Protein Traffic, Membrane Contact Sites and Innate Immunity

Kreimendahl

Rassow

2020

IJMS

View full text Add to dashboard Cite

Tom70 is a versatile adaptor protein of 70 kDa anchored in the outer membrane of mitochondria in metazoa, fungi and amoeba. The tertiary structure was resolved for the Tom70 of yeast, showing 26 α-helices, most of them participating in the formation of 11 tetratricopeptide repeat (TPR) motifs. Tom70 serves as a docking site for cytosolic chaperone proteins and co-chaperones and is thereby involved in the uptake of newly synthesized chaperone-bound proteins in mitochondrial biogenesis. In yeast, Tom70 additionally mediates ER-mitochondria contacts via binding to sterol transporter Lam6/Ltc1. In mammalian cells, TOM70 promotes endoplasmic reticulum (ER) to mitochondria Ca2+ transfer by association with the inositol-1,4,5-triphosphate receptor type 3 (IP3R3). TOM70 is specifically targeted by the Bcl-2-related protein MCL-1 that acts as an anti-apoptotic protein in macrophages infected by intracellular pathogens, but also in many cancer cells. By participating in the recruitment of PINK1 and the E3 ubiquitin ligase Parkin, TOM70 can be implicated in the development of Parkinson’s disease. TOM70 acts as receptor of the mitochondrial antiviral-signaling protein (MAVS) and thereby participates in the corresponding system of innate immunity against viral infections. The protein encoded by Orf9b in the genome of SARS-CoV-2 binds to TOM70, probably compromising the synthesis of type I interferons.

show abstract

“…Whether it occurs cotranslational or posttranslationally, the import of proteins into mitochondria is a particularly challenging problem that eukaryotes needed to "solve", due to the complex architecture of the mitochondria, requiring the bridging of two membrane delineated spaces i.e. the intermembrane space and matrix (Wojtkowska et al, 2015). The reference model of mitochondrial import machinery is that of Saccharomyces cerevisiae (Demishtein-Zohary and Azem, 2017).…”

Section: Protein Importmentioning

confidence: 99%

The Dictyostelium model for mitochondrial biology and disease

Pearce¹,

Annesley²,

Fisher³

2019

Int. J. Dev. Biol.

View full text Add to dashboard Cite

The unicellular slime mould Dictyostelium discoideum is a valuable eukaryotic model organism in the study of mitochondrial biology and disease. As a member of the Amoebozoa, a sister clade to the animals and fungi, Dictyostelium mitochondrial biology shares commonalities with these organisms, but also exhibits some features of plants. As such it has made significant contributions to the study of eukaryotic mitochondrial biology. This review provides an overview of the advances in mitochondrial biology made by the study of Dictyostelium and examines several examples where Dictyostelium has and will contribute to the understanding of mitochondrial disease. The study of Dictyostelium's mitochondrial biology has contributed to the understanding of mitochondrial genetics, transcription, protein import, respiration, morphology and trafficking, and the role of mitochondria in cellular differentiation. Dictyostelium is also proving to be a versatile model organism in the study both of classical mitochondrial disease e.g. Leigh syndrome, and in mitochondria-associated neurodegenerative diseases like Parkinson's disease. The study of mitochondrial diseases presents a unique challenge due to the cryptic nature of their genotypephenotype relationship. The use of Dictyostelium can contribute to resolving this problem by providing a genetically tractable, haploid eukaryotic organism with a suite of readily characterised phenotype readouts of cellular signalling pathways. Dictyostelium has provided insight into the signalling pathways involved in multiple neurodegenerative diseases and will continue to provide a significant contribution to the understanding of mitochondrial biology and disease.

show abstract

The TOM Complex of Amoebozoans: the Cases of the Amoeba Acanthamoeba castellanii and the Slime Mold Dictyostelium discoideum

Cited by 17 publications

References 65 publications

Origin and Evolutionary Alteration of the Mitochondrial Import System in Eukaryotic Lineages

Origin and Evolutionary Alteration of the Mitochondrial Import System in Eukaryotic Lineages

The Mitochondrial Outer Membrane Protein Tom70-Mediator in Protein Traffic, Membrane Contact Sites and Innate Immunity

The Dictyostelium model for mitochondrial biology and disease

Contact Info

Product

Resources

About