المؤلفون: Koparde, Pankaj, Mehta, Prachi, Reddy, Sushma, Ramakrishnan, Uma, Mukherjee, Shomita, Robin, V. V.

المصدر: PLoS ONE; 2/5/2018, Vol. 13 Issue 2, p1-15, 15p

مصطلحات موضوعية: PYGMY owls, RARE birds, PHYLOGENETIC models, MITOCHONDRIA, MITOSOMES

مستخلص: Range-restricted species generally have specific niche requirements and may often have unique evolutionary histories. Unfortunately, many of these species severely lack basic research, resulting in poor conservation strategies. The phylogenetic relationship of the Critically Endangered Forest Owlet Heteroglaux blewitti has been the subject of a century-old debate. The current classifications based on non-phylogenetic comparisons of morphology place the small owls of Asia into three genera, namely, Athene, Glaucidium, and Heteroglaux. Based on morphological and anatomical data, H. blewitti has been alternatively hypothesized to belong within Athene, Glaucidium, or its own monotypic genus Heteroglaux. To test these competing hypotheses, we sequenced six loci (~4300 bp data) and performed phylogenetic analyses of owlets. Mitochondrial and nuclear trees were not congruent in their placement of H. blewitti. However, both mitochondrial and nuclear combined datasets showed strong statistical support with high maximum likelihood bootstrap (>/ = 90) and Bayesian posterior probability values (>/ = 0.98) for H. blewitti being nested in the currently recognized Athene group, but not sister to Indian A. brama. The divergence of H. blewitti from its sister taxa was between 4.3 and 5.7 Ma coinciding with a period of drastic climatic changes in the Indian subcontinent. This study presented the first genetic analysis of H. blewitti, a Critically Endangered species, and addressed the long debate on the relationships of the Athene-Heteroglaux-Glaucidium complex. We recommend further studies with more data and complete taxon sampling to understand the biogeography of Indian Athene species. [ABSTRACT FROM AUTHOR]

: Copyright of PLoS ONE is the property of Public Library of Science and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Rout, Samuel, Zumthor, Jon Paulin, Schraner, Elisabeth M., Faso, Carmen, Hehl, Adrian B.

المصدر: PLoS Pathogens; 12/7/2016, Vol. 12 Issue 12, p1-32, 32p

مصطلحات موضوعية: GIARDIA lamblia, PROTEINS, PARASITES, MITOSOMES, HOMEOSTASIS, ENDOPLASMIC reticulum

مستخلص: Protozoan parasites of the genus Giardia are highly prevalent globally, and infect a wide range of vertebrate hosts including humans, with proliferation and pathology restricted to the small intestine. This narrow ecological specialization entailed extensive structural and functional adaptations during host-parasite co-evolution. An example is the streamlined mitosomal proteome with iron-sulphur protein maturation as the only biochemical pathway clearly associated with this organelle. Here, we applied techniques in microscopy and protein biochemistry to investigate the mitosomal membrane proteome in association to mitosome homeostasis. Live cell imaging revealed a highly immobilized array of 30–40 physically distinct mitosome organelles in trophozoites. We provide direct evidence for the single giardial dynamin-related protein as a contributor to mitosomal morphogenesis and homeostasis. To overcome inherent limitations that have hitherto severely hampered the characterization of these unique organelles we applied a novel interaction-based proteome discovery strategy using forward and reverse protein co-immunoprecipitation. This allowed generation of organelle proteome data strictly in a protein-protein interaction context. We built an initial Tom40-centered outer membrane interactome by co-immunoprecipitation experiments, identifying small GTPases, factors with dual mitosome and endoplasmic reticulum (ER) distribution, as well as novel matrix proteins. Through iterative expansion of this protein-protein interaction network, we were able to i) significantly extend this interaction-based mitosomal proteome to include other membrane-associated proteins with possible roles in mitosome morphogenesis and connection to other subcellular compartments, and ii) identify novel matrix proteins which may shed light on mitosome-associated metabolic functions other than Fe-S cluster biogenesis. Functional analysis also revealed conceptual conservation of protein translocation despite the massive divergence and reduction of protein import machinery in Giardia mitosomes. [ABSTRACT FROM AUTHOR]

: Copyright of PLoS Pathogens is the property of Public Library of Science and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Verena Zimorski, Aloysius G.M. Tielens, William Martin, Marek Mentel

المساهمون: Medical Microbiology & Infectious Diseases

المصدر: Free Radical Biology and Medicine
Free Radical Biology & Medicine
Free Radical Biology and Medicine, 140, 279-294. Elsevier Inc.

مصطلحات موضوعية: 0301 basic medicine, Hydrogenosome, Earth history, chemistry.chemical_element, Great oxidation event, Biochemistry, Euglena, Oxygen, Hydrogenosomes, Article, 03 medical and health sciences, 0302 clinical medicine, Physiology (medical), Botany, Mitosomes, Anaerobiosis, Oxidase test, biology, Chemistry, Atmosphere, Great Oxygenation Event, Chlamydomonas, Eukaryota, Metabolism, biology.organism_classification, Anoxic waters, Biological Evolution, Mitochondria, 030104 developmental biology, Eukaryote anaerobes, 13. Climate action, Energy Metabolism, Anaerobic exercise, 030217 neurology & neurosurgery

الوصف: Eukaryotes arose about 1.6 billion years ago, at a time when oxygen levels were still very low on Earth, both in the atmosphere and in the ocean. According to newer geochemical data, oxygen rose to approximately its present atmospheric levels very late in evolution, perhaps as late as the origin of land plants (only about 450 million years ago). It is therefore natural that many lineages of eukaryotes harbor, and use, enzymes for oxygen-independent energy metabolism. This paper provides a concise overview of anaerobic energy metabolism in eukaryotes with a focus on anaerobic energy metabolism in mitochondria. We also address the widespread assumption that oxygen improves the overall energetic state of a cell. While it is true that ATP yield from glucose or amino acids is increased in the presence of oxygen, it is also true that the synthesis of biomass costs thirteen times more energy per cell in the presence of oxygen than in anoxic conditions. This is because in the reaction of cellular biomass with O2, the equilibrium lies very far on the side of CO2. The absence of oxygen offers energetic benefits of the same magnitude as the presence of oxygen. Anaerobic and low oxygen environments are ancient. During evolution, some eukaryotes have specialized to life in permanently oxic environments (life on land), other eukaryotes have remained specialized to low oxygen habitats. We suggest that the Km of mitochondrial cytochrome c oxidase of 0.1–10 μM for O2, which corresponds to about 0.04%–4% (avg. 0.4%) of present atmospheric O2 levels, reflects environmental O2 concentrations that existed at the time that the eukaryotes arose.
Graphical abstract Image 1
Highlights • The first 1.5 billion years of life history took place without molecular oxygen. • The first eukaryotes appeared ca. 1.6 billion years ago, oxygen rose with land plants. • Eukaryotes arose and diversified with low oxygen, anaerobic ATP synthesis is ancient. • Anaerobic energy metabolism in mitochondria is common among eukaryotic lineages. • The Km of cytochrome c oxidase might reflect low environmental O2 at eukaryote origin.

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::772cdd011718b506aa9577f56c9d5d91Test
https://hdl.handle.net/1765/121103Test

المؤلفون: Zubáčová, Zuzana, Novák, Lukáš, Bublíková, Jitka, Vacek, Vojtěch, Fousek, Jan, Rídl, Jakub, Tachezy, Jan, Doležal, Pavel, Vlček, Čestmír, Hampl, Vladimír

المصدر: PLoS ONE; Mar2013, Vol. 8 Issue 3, p1-9, 9p

مصطلحات موضوعية: MITOCHONDRIA, EUKARYOTES, ENDOSYMBIOSIS, MITOSOMES, BIOLOGICAL evolution, SEQUENCE alignment, GENETIC transcription, AMINO acid metabolism

مستخلص: All eukaryotic organisms contain mitochondria or organelles that evolved from the same endosymbiotic event like classical mitochondria. Organisms inhabiting low oxygen environments often contain mitochondrial derivates known as hydrogenosomes, mitosomes or neutrally as mitochondrion-like organelles. The detailed investigation has shown unexpected evolutionary plasticity in the biochemistry and protein composition of these organelles in various protists. We investigated the mitochondrion-like organelle in Trimastix pyriformis, a free-living member of one of the three lineages of anaerobic group Metamonada. Using 454 sequencing we have obtained 7 037 contigs from its transcriptome and on the basis of sequence homology and presence of N-terminal extensions we have selected contigs coding for proteins that putatively function in the organelle. Together with the results of a previous transcriptome survey, the list now consists of 23 proteins – mostly enzymes involved in amino acid metabolism, transporters and maturases of proteins and transporters of metabolites. We have no evidence of the production of ATP in the mitochondrion-like organelle of Trimastix but we have obtained experimental evidence for the presence of enzymes of the glycine cleavage system (GCS), which is part of amino acid metabolism. Using homologous antibody we have shown that H-protein of GCS localizes into vesicles in the cell of Trimastix. When overexpressed in yeast, H- and P-protein of GCS and cpn60 were transported into mitochondrion. In case of H-protein we have demonstrated that the first 16 amino acids are necessary for this transport. Glycine cleavage system is at the moment the only experimentally localized pathway in the mitochondrial derivate of Trimastix pyriformis. [ABSTRACT FROM AUTHOR]

: Copyright of PLoS ONE is the property of Public Library of Science and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Jan Tachezy, Sriram G. Garg, William Martin, Sven B. Gould, Verena Zimorski, Jan Stölting, Petr Rada

المصدر: Genome Biology and Evolution

مصطلحات موضوعية: Saccharomyces cerevisiae Proteins, TIM/TOM complex, Saccharomyces cerevisiae, Protein Sorting Signals, Mitochondrion, Biology, medicine.disease_cause, Evolution, Molecular, Mitochondrial Proteins, Transit Peptide, Protein targeting, Trichomonas vaginalis, Genetics, medicine, Inner mitochondrial membrane, Ecology, Evolution, Behavior and Systematics, mitosomes, Mitochondrial carrier, Translocon, Mitochondria, Transport protein, Protein Transport, TOM/TIM, Biochemistry, hydrogenosomes, protein import, Research Article

الوصف: The origin of protein import was a key step in the endosymbiotic acquisition of mitochondria. Though the main translocon of the mitochondrial outer membrane, TOM40, is ubiquitous among organelles of mitochondrial ancestry, the transit peptides, or N-terminal targeting sequences (NTSs), recognised by the TOM complex, are not. To better understand the nature of evolutionary conservation in mitochondrial protein import, we investigated the targeting behavior of Trichomonas vaginalis hydrogenosomal proteins in Saccharomyces cerevisiae and vice versa. Hydrogenosomes import yeast mitochondrial proteins even in the absence of their native NTSs, but do not import yeast cytosolic proteins. Conversely, yeast mitochondria import hydrogenosomal proteins with and without their short NTSs. Conservation of an NTS-independent mitochondrial import route from excavates to opisthokonts indicates its presence in the eukaryote common ancestor. Mitochondrial protein import is known to entail electrophoresis of positively charged NTSs across the electrochemical gradient of the inner mitochondrial membrane. Our present findings indicate that mitochondrial transit peptides, which readily arise from random sequences, were initially selected as a signal for charge-dependent protein targeting specifically to the mitochondrial matrix. Evolutionary loss of the electron transport chain in hydrogenosomes and mitosomes lifted the selective constraints that maintain positive charge in NTSs, allowing first the NTS charge, and subsequently the NTS itself, to be lost. This resulted in NTS-independent matrix targeting, which is conserved across the evolutionary divide separating trichomonads and yeast, and which we propose is the ancestral state of mitochondrial protein import.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14702a1d9da2d81747fd4617be1b484eTest
https://doi.org/10.1093/gbe/evv175Test

المؤلفون: Jan Tachezy, Maximiliano G. De Napoli, Luboš Voleman, Daria Van Tyne, Christine S. Hopp, Michaela Marcinčiková, Vladimíra Najdrová, Eva Martincová, Pavel Doležal, David E. Sanin, Dawn M. Walker, Shiri Eshar, Melisa Gualdron, Dumizulu L. Tembo

المساهمون: UCL - SSS/DDUV - Institut de Duve

المصدر: PLoS ONE, Vol 7, Iss 4, p e36314 (2012)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE
PLoS One, Vol. 7, no. 4 (2012)

مصطلحات موضوعية: Hydrolases, Hydrogenosome, Protozoan Proteins, lcsh:Medicine, Mitosome, Protozoology, Ligands, medicine.disease_cause, Biochemistry, purl.org/becyt/ford/1 [https], Genes, Reporter, Molecular Cell Biology, Anaerobiosis, lcsh:Science, 0303 health sciences, Multidisciplinary, biology, Cellular Structures, Mitochondria, Molecular Imaging, 3. Good health, Cell biology, hydrogenosomes, Cytochemistry, CIENCIAS NATURALES Y EXACTAS, Research Article, Cell Survival, Recombinant Fusion Proteins, Otras Ciencias Biológicas, Genetic Vectors, Microbiology, Ciencias Biológicas, 03 medical and health sciences, Eukaryotic Evolution, Live cell imaging, Organelle, Trichomonas vaginalis, medicine, Giardia lamblia, Parasite Evolution, purl.org/becyt/ford/1.6 [https], Biology, 030304 developmental biology, Live imaging, Organelles, Evolutionary Biology, 030306 microbiology, lcsh:R, mitosomes, Organismal Evolution, Subcellular Organelles, Frataxin, biology.protein, Parastic Protozoans, Parasitology, lcsh:Q, ISCU, Halo tags

الوصف: Hydrogenosomes and mitosomes represent remarkable mitochondrial adaptations in the anaerobic parasitic protists such as Trichomonas vaginalis and Giardia intestinalis, respectively. In order to provide a tool to study these organelles in the live cells, the HaloTag was fused to G. intestinalis IscU and T. vaginalis frataxin and expressed in the mitosomes and hydrogenosomes, respectively. The incubation of the parasites with the fluorescent Halo-ligand resulted in highly specific organellar labeling, allowing live imaging of the organelles. With the array of available ligands the HaloTag technology offers a new tool to study the dynamics of mitochondria-related compartments as well as other cellular components in these intriguing unicellular eukaryotes. Fil: Martincová, Eva. Charles University; República Checa Fil: Voleman, Luboš. Charles University; República Checa Fil: Najdrová, Vladimíra. Charles University; República Checa Fil: de Napoli, Maximiliano Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina Fil: Eshar, Shiri. Hebrew University-Hadassah Medical School; Israel Fil: Gualdron, Melisa. Christian De Duve Institute of Cellular Pathology; Bélgica Fil: Hopp, Christine S.. School of Hygiene and Tropical Medicine. Malaria Centre; Reino Unido Fil: Sanin, David E.. University of York; Reino Unido Fil: Tembo, Dumizulu L.. Malawi-Liverpool Wellcome Trust Clinical Research Programme; Malaui Fil: Van Tyne, Daria. Harvard University. Harvard School of Public Health; Estados Unidos Fil: Walker, Dawn. Integrated Biomedical Sciences Center for Microbial Interface Biology Department of Internal Medicine; Estados Unidos Fil: Marcinčiková, Michaela. Charles University; República Checa Fil: Tachezy, Jan. Charles University; República Checa Fil: Doležal, Pavel. Charles University; República Checa

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fecb00c39c3a37621d576079ff181b09Test
http://europepmc.org/articles/PMC3338651?pdf=renderTest