The Mitochondrial Complexome of Medicago truncatula

Abstract

Legumes (Fabaceae, Leguminosae) are unique in their ability to carry out an elaborate endosymbiotic nitrogen fixation process with rhizobia proteobacteria. The symbiotic nitrogen fixation enables the host plants to grow almost independently of any other nitrogen source. Establishment of symbiosis requires adaptations of the host cellular metabolism, here foremost of the energy metabolism mainly taking place in mitochondria. Since the early 1990s, the galegoid legume Medicago truncatula Gaertn. is a well-established model for studying legume biology, but little is known about the protein complement of mitochondria from this species. An initial characterization of the mitochondrial proteome of M. truncatula (Jemalong A17) was published recently. In the frame of this study, mitochondrial protein complexes were characterized using Two-dimensional (2D) Blue native (BN)/SDS-PAGE. From 139 detected spots, the “first hit” (=most abundant) proteins of 59 spots were identified by mass spectrometry. Here, we present a comprehensive analysis of the mitochondrial “complexome” (the “protein complex proteome”) of M. truncatula via 2D BN/SDS-PAGE in combination with highly sensitive MS protein identification. In total, 1,485 proteins were identified within 158 gel spots, representing 467 unique proteins. Data evaluation by the novel GelMap annotation tool allowed recognition of protein complexes of low abundance. Overall, at least 36 mitochondrial protein complexes were found. To our knowledge several of these complexes were described for the first time in Medicago. The data set is accessible under . The mitochondrial protein complex proteomes of Arabidopsis available at and Medicago are compared.

The Complexome of Dehalococcoides mccartyi Reveals Its Organohalide Respiration-Complex Is Modular

“…By identifying correlating distribution patterns, evidence for protein-protein interactions and the formation of protein complexes can be obtained. The method was described before for mitochondrial complexes in mammals (Wittig et al, 2006 ; Heide et al, 2012 ), plants (Kiirika et al, 2013 ; Senkler et al, 2017 ), and yeast (Eydt et al, 2017 ), and bacterial protein complexes of sulfate-reducing (Wöhlbrand et al, 2016 ), oxygen respiration in nitrate-reducing (Schimo et al, 2017 ) and anammox bacteria (de Almeida et al, 2016 ). A complication of complexome analyses is the fact that many of the protein complexes, especially those involved in respiration, are membrane bound and detergents must be applied to detach protein complexes from the membrane.…”

Subcellular proteomics—where cell biology meets protein chemistry

“…We have brought together a wide array of 26 publications including original research articles, reviews, and mini-reviews. They are focused on the model plants Arabidopsis (Parsons et al, 2012 ; Albenne et al, 2013 ; Bussell et al, 2013 ; Carroll, 2013 ; Lee et al, 2013a ; Peters et al, 2013 ; Simm et al, 2013 ; Yadeta et al, 2013 ; Ito et al, 2014 ), rice (Huang et al, 2013 ; Komatsu and Yanagawa, 2013 ) and medicago (Kiirika et al, 2013 ; Lee et al, 2013b ; Simm et al, 2013 ) as well as crop plants wheat, barley, maize, and tomato (Casati, 2012 ; Komatsu and Yanagawa, 2013 ; Petersen et al, 2013 ; Ruiz-May and Rose, 2013 ; Zhang et al, 2013 ). They include studies of the easily isolated subcellular proteomes of the chloroplast, mitochondria, peroxisome, and nuclei (Casati, 2012 ; Repetto et al, 2012 ; Bussell et al, 2013 ; Havelund et al, 2013 ; Huang et al, 2013 ; Lee et al, 2013a ; Narula et al, 2013 ; Peters et al, 2013 ; Petersen et al, 2013 ; Simm et al, 2013 ), as well as less easily isolated golgi, plasma membrane, cytosolic ribosome, and cell wall proteomes(Parsons et al, 2012 ; Carroll, 2013 ; Takahashi et al, 2013 ; Yadeta et al, 2013 ; Zhang et al, 2013 ).…”

Mitochondrial сomplexome of etiolated pea shoots

“…рисунок). В нашем исследовании олигомеры порина были обнаружены в виде диффузных пятен в области 80-90 и 130-150 кДа, что согласуется с данными других исследователей, которые дополнительно детектировали олигомеры VDAC с большей молекулярной массой [19,20]. Три изоформы АДФ/АТФ-транслокатора и переносчик дикарбоксилатов локализуются в одном пятне (п60) в области 90 кДа, что может предполагать олигомерное состояние этих белков.…”