scholarly journals There Is Treasure Everywhere: Reductive Plastid Evolution in Apicomplexa in Light of Their Close Relatives

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 378 ◽  
Author(s):  
Eric Salomaki ◽  
Martin Kolisko
Keyword(s):  
Evolutionary History ◽  
Acid Synthesis ◽  
Plastid Evolution ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Intracellular Parasites ◽  
History Of ◽  
Close Relatives ◽  
Generation Sequencing ◽  
Core Genes

The phylum Apicomplexa (Alveolates) comprises a group of host-associated protists, predominately intracellular parasites, including devastating parasites like Plasmodium falciparum, the causative agent of malaria. One of the more fascinating characteristics of Apicomplexa is their highly reduced (and occasionally lost) remnant plastid, termed the apicoplast. Four core metabolic pathways are retained in the apicoplast: heme synthesis, iron–sulfur cluster synthesis, isoprenoid synthesis, and fatty acid synthesis. It has been suggested that one or more of these pathways are essential for plastid and plastid genome retention. The past decade has witnessed the discovery of several apicomplexan relatives, and next-generation sequencing efforts are revealing that they retain variable plastid metabolic capacities. These data are providing clues about the core genes and pathways of reduced plastids, while at the same time further confounding our view on the evolutionary history of the apicoplast. Here, we examine the evolutionary history of the apicoplast, explore plastid metabolism in Apicomplexa and their close relatives, and propose that the differences among reduced plastids result from a game of endosymbiotic roulette. Continued exploration of the Apicomplexa and their relatives is sure to provide new insights into the evolution of the apicoplast and apicomplexans as a whole.

scholarly journals A Review of Multiple Mitochondrial Dysfunction Syndromes, Syndromes Associated with Defective Fe-S Protein Maturation

Biomedicines ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 989
Author(s):  
Elise Lebigot ◽  
Manuel Schiff ◽  
Marie-Pierre Golinelli-Cohen
Keyword(s):  
Mitochondrial Dysfunction ◽  
Acid Synthesis ◽  
Large Gene ◽  
Iron Sulfur ◽  
Whole Exome ◽  
Radiological Data ◽  
Cellular Pathways ◽  
Gene Panels ◽  
Generation Sequencing

Mitochondrial proteins carrying iron-sulfur (Fe-S) clusters are involved in essential cellular pathways such as oxidative phosphorylation, lipoic acid synthesis, and iron metabolism. NFU1, BOLA3, IBA57, ISCA2, and ISCA1 are involved in the last steps of the maturation of mitochondrial [4Fe-4S]-containing proteins. Since 2011, mutations in their genes leading to five multiple mitochondrial dysfunction syndromes (MMDS types 1 to 5) were reported. The aim of this systematic review is to describe all reported MMDS-patients. Their clinical, biological, and radiological data and associated genotype will be compared to each other. Despite certain specific clinical elements such as pulmonary hypertension or dilated cardiomyopathy in MMDS type 1 or 2, respectively, nearly all of the patients with MMDS presented with severe and early onset leukoencephalopathy. Diagnosis could be suggested by high lactate, pyruvate, and glycine levels in body fluids. Genetic analysis including large gene panels (Next Generation Sequencing) or whole exome sequencing is needed to confirm diagnosis.

scholarly journals Evolutionary History of Contagious Bovine Pleuropneumonia Using Next Generation Sequencing of Mycoplasma mycoides Subsp. mycoides “Small Colony”

PLoS ONE ◽  
2012 ◽  
Vol 7 (10) ◽  
pp. e46821 ◽  
Author(s):  
Virginie Dupuy ◽  
Lucía Manso-Silván ◽  
Valérie Barbe ◽  
Patricia Thebault ◽  
Emilie Dordet-Frisoni ◽  
...  
Keyword(s):  
Next Generation Sequencing ◽  
Evolutionary History ◽  
Next Generation ◽  
Contagious Bovine Pleuropneumonia ◽  
Mycoplasma Mycoides ◽  
History Of ◽  
Small Colony ◽  
Generation Sequencing

scholarly journals Evolution of the Cytosolic Iron-Sulfur Cluster Assembly Machinery in Blastocystis Species and Other Microbial Eukaryotes

2013 ◽  
Vol 13 (1) ◽  
pp. 143-153 ◽  
Author(s):  
Anastasios D. Tsaousis ◽  
Eleni Gentekaki ◽  
Laura Eme ◽  
Daniel Gaston ◽  
Andrew J. Roger
Keyword(s):  
Subcellular Fractionation ◽  
Comparative Genomic ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Content Type ◽  
Sulfur Cluster ◽  
Evolutionary Diversification ◽  
Iron Sulfur ◽  
History Of ◽  
Phylogenomic Analyses

ABSTRACT The cytosolic iron/sulfur cluster assembly (CIA) machinery is responsible for the assembly of cytosolic and nuclear iron/sulfur clusters, cofactors that are vital for all living cells. This machinery is uniquely found in eukaryotes and consists of at least eight proteins in opisthokont lineages, such as animals and fungi. We sought to identify and characterize homologues of the CIA system proteins in the anaerobic stramenopile parasite Blastocystis sp. strain NandII. We identified transcripts encoding six of the components—Cia1, Cia2, MMS19, Nbp35, Nar1, and a putative Tah18—and showed using immunofluorescence microscopy, immunoelectron microscopy, and subcellular fractionation that the last three of them localized to the cytoplasm of the cell. We then used comparative genomic and phylogenetic approaches to investigate the evolutionary history of these proteins. While most Blastocystis homologues branch with their eukaryotic counterparts, the putative Blastocystis Tah18 seems to have a separate evolutionary origin and therefore possibly a different function. Furthermore, our phylogenomic analyses revealed that all eight CIA components described in opisthokonts originated before the diversification of extant eukaryotic lineages and were likely already present in the last eukaryotic common ancestor (LECA). The Nbp35, Nar1 Cia1, and Cia2 proteins have been conserved during the subsequent evolutionary diversification of eukaryotes and are present in virtually all extant lineages, whereas the other CIA proteins have patchy phylogenetic distributions. Cia2 appears to be homologous to SufT, a component of the prokaryotic sulfur utilization factors (SUF) system, making this the first reported evolutionary link between the CIA and any other Fe/S biogenesis pathway. All of our results suggest that the CIA machinery is an ubiquitous biosynthetic pathway in eukaryotes, but its apparent plasticity in composition raises questions regarding how it functions in nonmodel organisms and how it interfaces with various iron/sulfur cluster systems (i.e., the iron/sulfur cluster, nitrogen fixation, and/or SUF system) found in eukaryotic cells.

Evolutionary history of the Eurasian steppe plant Schivereckia podolica (Brassicaceae) and its close relatives

Flora ◽  
2020 ◽  
Vol 268 ◽  
pp. 151602 ◽  
Author(s):  
Nikolai Friesen ◽  
Anže Zerdoner Calasan ◽  
Barbara Neuffer ◽  
Dmitry A. German ◽  
Michael Markov ◽  
...  
Keyword(s):  
Evolutionary History ◽  
Eurasian Steppe ◽  
History Of ◽  
Steppe Plant ◽  
Close Relatives

scholarly journals The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Jonathan G Van Vranken ◽  
Mi-Young Jeong ◽  
Peng Wei ◽  
Yu-Chan Chen ◽  
Steven P Gygi ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acyl Carrier Protein ◽  
Acyl Chain ◽  
Acid Synthesis ◽  
Carrier Protein ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Mitochondrial Fatty Acid

Mitochondrial fatty acid synthesis (FASII) and iron sulfur cluster (FeS) biogenesis are both vital biosynthetic processes within mitochondria. In this study, we demonstrate that the mitochondrial acyl carrier protein (ACP), which has a well-known role in FASII, plays an unexpected and evolutionarily conserved role in FeS biogenesis. ACP is a stable and essential subunit of the eukaryotic FeS biogenesis complex. In the absence of ACP, the complex is destabilized resulting in a profound depletion of FeS throughout the cell. This role of ACP depends upon its covalently bound 4’-phosphopantetheine (4-PP)-conjugated acyl chain to support maximal cysteine desulfurase activity. Thus, it is likely that ACP is not simply an obligate subunit but also exploits the 4-PP-conjugated acyl chain to coordinate mitochondrial fatty acid and FeS biogenesis.

scholarly journals Fundamental Difficulties Prevent the Reconstruction of the Deep Phylogeny of Viruses

Viruses ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 1130 ◽  
Author(s):  
Jean-Michel Claverie
Keyword(s):  
Evolutionary History ◽  
Large Scale ◽  
Environmental Virology ◽  
Fundamental Limitations ◽  
Intracellular Parasites ◽  
Virion Structure ◽  
Agricultural Applications ◽  
History Of ◽  
High Level ◽  
Biological Entities

The extension of virology beyond its traditional medical, veterinary, or agricultural applications, now called environmental virology, has shown that viruses are both the most numerous and diverse biological entities on Earth. In particular, virus isolations from unicellular eukaryotic hosts (heterotrophic and photosynthetic protozoans) revealed numerous viral types previously unexpected in terms of virion structure, gene content, or mode of replication. Complemented by large-scale metagenomic analyses, these discoveries have rekindled interest in the enigma of the origin of viruses, for which a description encompassing all their diversity remains not available. Several laboratories have repeatedly tackled the deep reconstruction of the evolutionary history of viruses, using various methods of molecular phylogeny applied to the few shared “core” genes detected in certain virus groups (e.g., the Nucleocytoviricota). Beyond the practical difficulties of establishing reliable homology relationships from extremely divergent sequences, I present here conceptual arguments highlighting several fundamental limitations plaguing the reconstruction of the deep evolutionary history of viruses, and even more the identification of their unique or multiple origin(s). These arguments also underline the risk of establishing premature high level viral taxonomic classifications. Those limitations are direct consequences of the random mechanisms governing the reductive/retrogressive evolution of all obligate intracellular parasites.

scholarly journals Anaerobic endosymbiont generates energy for ciliate host by denitrification

Nature ◽  
2021 ◽  
Author(s):  
Jon S. Graf ◽  
Sina Schorn ◽  
Katharina Kitzinger ◽  
Soeren Ahmerkamp ◽  
Christian Woehle ◽  
...  
Keyword(s):  
Tricarboxylic Acid Cycle ◽  
Iron Sulfur Cluster ◽  
Terminal Oxidases ◽  
Iron Sulfur ◽  
Obligate Anaerobic ◽  
Transport Chain ◽  
Anaerobic Ciliate ◽  
Atp Generation ◽  
Cluster Biosynthesis ◽  
Core Genes

AbstractMitochondria are specialized eukaryotic organelles that have a dedicated function in oxygen respiration and energy production. They evolved about 2 billion years ago from a free-living bacterial ancestor (probably an alphaproteobacterium), in a process known as endosymbiosis1,2. Many unicellular eukaryotes have since adapted to life in anoxic habitats and their mitochondria have undergone further reductive evolution3. As a result, obligate anaerobic eukaryotes with mitochondrial remnants derive their energy mostly from fermentation4. Here we describe ‘Candidatus Azoamicus ciliaticola’, which is an obligate endosymbiont of an anaerobic ciliate and has a dedicated role in respiration and providing energy for its eukaryotic host. ‘Candidatus A. ciliaticola’ contains a highly reduced 0.29-Mb genome that encodes core genes for central information processing, the electron transport chain, a truncated tricarboxylic acid cycle, ATP generation and iron–sulfur cluster biosynthesis. The genome encodes a respiratory denitrification pathway instead of aerobic terminal oxidases, which enables its host to breathe nitrate instead of oxygen. ‘Candidatus A. ciliaticola’ and its ciliate host represent an example of a symbiosis that is based on the transfer of energy in the form of ATP, rather than nutrition. This discovery raises the possibility that eukaryotes with mitochondrial remnants may secondarily acquire energy-providing endosymbionts to complement or replace functions of their mitochondria.

scholarly journals Mitochondria, oxidative stress and the petite phenotype in Saccharomyces cerevisiae

2010 ◽  
Vol 31 (2) ◽  
pp. 82
Author(s):  
Anita Ayer ◽  
Ian W Dawes ◽  
Gabriel G Perrone
Keyword(s):  
Oxidative Stress ◽  
Energy Production ◽  
Acid Synthesis ◽  
Nuclear Space ◽  
Amino Acid Synthesis ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Eukaryotic Organisms ◽  
State Concentration

Oxidative stress has long been recognised as biologically important and is increasingly implicated in a variety of phenomena, such as mutation, carcinogenesis, degenerative and other diseases, inflammation, ageing, and development. The role of the mitochondrion in oxidative stress and the production of reactive oxygen species (ROS) and other radical species is well-established, with mitochondria providing a fascinating area of study within the oxidative stress field. Mitochondria are essential organelles for the viability of all eukaryotic organisms. While mitochondria perform important processes associated with oxidative phosphorylation and energy production, and numerous other metabolic processes, such as iron sulfur cluster biogenesis, lipid and amino acid synthesis, they also appear to be the largest intracellular source of ROS in aerobic cells. The steady state concentration of O2 in the mitochondrial matrix is five- to tenfold higher than in the cytosol or nuclear space according to one estimation. Therefore, mitochondrial macromolecules such as mitochondrial DNA are particularly susceptible to oxidative damage.

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