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  1. Alternating terminal electron-acceptors at the basis of symbiogenesis: How oxygen ignited eukaryotic evolution.Dave Speijer - 2017 - Bioessays 39 (2):1600174.
    What kind of symbiosis between archaeon and bacterium gave rise to their eventual merger at the origin of the eukaryotes? I hypothesize that conditions favouring bacterial uptake were based on exchange of intermediate carbohydrate metabolites required by recurring changes in availability and use of the two different terminal electron chain acceptors, the bacterial one being oxygen. Oxygen won, and definitive loss of the archaeal membrane potential allowed permanent establishment of the bacterial partner as the proto‐mitochondrion, further metabolic integration and highly (...)
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  • Birth of the eukaryotes by a set of reactive innovations: New insights force us to relinquish gradual models.Dave Speijer - 2015 - Bioessays 37 (12):1268-1276.
    Of two contending models for eukaryotic evolution the “archezoan“ has an amitochondriate eukaryote take up an endosymbiont, while “symbiogenesis“ states that an Archaeon became a eukaryote as the result of this uptake. If so, organelle formation resulting from new engulfments is simplified by the primordial symbiogenesis, and less informative regarding the bacterium‐to‐mitochondrion conversion. Gradualist archezoan visions still permeate evolutionary thinking, but are much less likely than symbiogenesis. Genuine amitochondriate eukaryotes have never been found and rapid, explosive adaptive periods characteristic of (...)
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  • The evolution of eukaryotic cells from the perspective of peroxisomes.Kathrin Bolte, Stefan A. Rensing & Uwe-G. Maier - 2015 - Bioessays 37 (2):195-203.
    Beta‐oxidation of fatty acids and detoxification of reactive oxygen species are generally accepted as being fundamental functions of peroxisomes. Additionally, these pathways might have been the driving force favoring the selection of this compartment during eukaryotic evolution. Here we performed phylogenetic analyses of enzymes involved in beta‐oxidation of fatty acids in Bacteria, Eukaryota, and Archaea. These imply an alpha‐proteobacterial origin for three out of four enzymes. By integrating the enzymes' history into the contrasting models on the origin of eukaryotic cells, (...)
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  • How the mitochondrion was shaped by radical differences in substrates.Dave Speijer - 2014 - Bioessays 36 (7):634-643.
    As free‐living organisms, alpha‐proteobacteria produce reactive oxygen species (ROS) that diffuse into the surroundings; once constrained inside the archaeal ancestor of eukaryotes, however, ROS production presented evolutionary pressures – especially because the alpha‐proteobacterial symbiont made more ROS, from a variety of substrates. I previously proposed that ratios of electrons coming from FADH2 and NADH (F/N ratios) correlate with ROS production levels during respiration, glucose breakdown having a much lower F/N ratio than longer fatty acid (FA) breakdown. Evidently, higher endogenous ROS (...)
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  • Oxygen radicals shaping evolution: Why fatty acid catabolism leads to peroxisomes while neurons do without it.Dave Speijer - 2011 - Bioessays 33 (2):88-94.
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  • Mitochondria and peroxisomes: Are the 'Big Brother' and the 'Little Sister' closer than assumed?Michael Schrader & Yisang Yoon - 2007 - Bioessays 29 (11):1105-1114.
    Mitochondria and peroxisomes are essential subcellular organelles in mammals. Despite obvious differences, both organelles display certain morphological and functional similarities. Recent studies have elucidated that these highly dynamic and plastic organelles share components of their division machinery. Mitochondria and peroxisomes are metabolically linked organelles, which are cooperating and cross‐talking. This review addresses the dynamics and division of mitochondria and peroxisomes as well as their functional similarities to provide insight as to why these organelles share the fission machinery in evolutionary aspects.© (...)
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  • Making new out of old: Recycling and modification of an ancient protein translocation system during eukaryotic evolution.Kathrin Bolte, Nicole Gruenheit, Gregor Felsner, Maik S. Sommer, Uwe-G. Maier & Franziska Hempel - 2011 - Bioessays 33 (5):368-376.
    At first glance the three eukaryotic protein translocation machineries – the ER‐associated degradation (ERAD) transport apparatus of the endoplasmic reticulum, the peroxisomal importomer and SELMA, the pre‐protein translocator of complex plastids – appear quite different. However, mechanistic comparisons and phylogenetic analyses presented here suggest that all three translocation machineries share a common ancestral origin, which highlights the recycling of pre‐existing components as an effective evolutionary driving force.Editor's suggested further reading in BioEssays ERAD ubiquitin ligases Abstract.
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