Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits

Millar, A. Harvey; Eubel, Holger; Jänsch, Lothar; Kruft, Volker; Heazlewood, Joshua L.; Braun, Hans‐Peter

doi:10.1007/s11103-004-2316-2

Cited by 177 publications

(150 citation statements)

References 67 publications

Supporting

Mentioning

145

Contrasting

Order By: Relevance

“…Lower on the gel are the three diffusely staining bands of the cytochrome c oxidase complex (complex IV). As has been observed in several plant species (45), CIV runs as a larger CIVa form and a slightly smaller CIVb form. These membrane complexes are all present following all treatments, and no significant changes in protein abundance could be detected by Progenesis spot/ band density analysis.…”

Section: Impact Of Environmental Stress On Plant Mitochondriasupporting

confidence: 74%

Differential Impact of Environmental Stresses on the Pea Mitochondrial Proteome

Taylor

Heazlewood²,

Day³

et al. 2005

Molecular & Cellular Proteomics

Self Cite

236

153

View full text Add to dashboard Cite

Exposure to adverse environmental conditions causes oxidative stress in many organisms, leading either to disease and debilitation or to response and tolerance. Mitochondria are a key site of oxidative stress and of cellular response and play important roles in cell survival. We analyzed the response of mitochondria in pea (Pisum sativum) plants to the common stresses associated with drought, cold, and herbicides. These treatments all altered photosynthetic and respiratory rates of pea leaves to various extents, but only herbicides significantly increased lipid peroxidation product accumulation. Mitochondria isolated from the stressed pea plants maintained their electron transport chain activity, but changes were evident in the abundance of uncoupling proteins, non-phosphorylating respiratory pathways, and oxidative modification of lipoic acid moieties on mitochondrial proteins. These data suggest that herbicide treatment placed a severe oxidative stress on mitochondria, whereas chilling and particularly drought were milder stresses. Detailed analysis of the soluble proteome of mitochondria by gel electrophoresis and mass spectrometry revealed differential degradation of key matrix enzymes during treatments with chilling being significantly more damaging than drought. Differential induction of heat shock proteins and specific losses of other proteins illustrated the diversity of response to these stresses at the protein level. Cross-species matching was required for mass spectrometry identification of nine proteins because only a limited number of pea cDNAs have been sequenced, and the full pea genome is not available. Blue-native separation of intact respiratory chain complexes revealed little if any change in response to environmental stresses. Together these data suggest that although many of the mo Cellular homeostasis can be disrupted by changes in the extracellular environment that uncouple biochemical pathways, which normally operate under a range of biophysical and chemical constraints. Such disruption is often accompanied by the undesirable accumulation of metabolic intermediates, and the most studied of these are reactive oxygen species (ROS) 1 produced by disruption of metabolism and electron transport chains. Much attention has focused on the impact of ROS during normal development and aging of cells and during perturbation of normal cellular life by disease, toxins, and the physical environment. Oxidative stress modification of proteins tends to increase with age in most organisms (1), but plants have recently been noted as an exception to the normal trend and are able to manage oxidative protein damage much more effectively during growth and later reproductive phases of life (2).Mitochondria form a focus for much oxidative stress research as not only are they the sites of oxygen consumption and a significant source of cellular ROS, but oxidative damage of the organelles perturbs the cell's energy supply required for repair mechanisms. Consequently the nature of oxidative damage to mitochondria is b...

show abstract

Section: Impact Of Environmental Stress On Plant Mitochondriasupporting

confidence: 74%

Differential Impact of Environmental Stresses on the Pea Mitochondrial Proteome

Taylor

Heazlewood²,

Day³

et al. 2005

Molecular & Cellular Proteomics

Self Cite

236

153

View full text Add to dashboard Cite

show abstract

“…However, recruitment of taxon-specific subunits is not limited to Euglenozoa, since unrelated additional subunits have also been described in A. thaliana (Millar et al, 2004).…”

Section: Complex IImentioning

confidence: 99%

The mitochondrial respiratory chain of the secondary green alga Euglena gracilis shares many additional subunits with parasitic Trypanosomatidae

et al. 2014

View full text Add to dashboard Cite

The mitochondrion is an essential organelle for the production of cellular ATP in most eukaryotic cells. It is extensively studied, including in parasitic organisms such as trypanosomes, as a potential therapeutic target. Recently, numerous additional subunits of the respiratory-chain complexes have been described in Trypanosoma brucei and Trypanosoma cruzi. Since these subunits had apparently no counterparts in other organisms, they were interpreted as potentially associated with the parasitic trypanosome lifestyle. Here we used two complementary approaches to characterise the subunit composition of respiratory complexes in Euglena gracilis, a non-parasitic secondary green alga related to trypanosomes. First, we developed a phylogenetic pipeline aimed at mining sequence databases for identifying homologs to known respiratory-complex subunits with high confidence. Second, we used MS/MS proteomics after two-dimensional separation of the respiratory complexes by Blue Native-and SDS-PAGE to both confirm in silico predictions and to identify further additional subunits. Altogether, we identified 41 subunits that are restricted to E. gracilis, T. brucei and T. cruzi, along with 48 classical subunits described in other eukaryotes (i.e. plants, mammals and fungi). This moreover demonstrates that at least half of the subunits recently reported in T. brucei and T. cruzi are actually not specific to Trypanosomatidae, but extend at least to other Euglenozoa, and that their origin and function are thus not specifically associated with the parasitic lifestyle. Furthermore, preliminary biochemical analyses suggest that some of these additional subunits underlie the peculiarities of the respiratory chain observed in Euglenozoa.Liège, february 06 th 2014Dear Editor, Please find the fully revised version of our manuscript "The mitochondrial respiratory chain of the secondary green alga Euglena gracilis shares many additional subunits with parasitic Trypanosomatidae."We are grateful to you for having encouraged us to resubmit a modified manuscript. We have addressed all the comments raised by the reviewers on our first submission. A point to point answer has been submitted along with the manuscript. Main changes are : (i) additional explanations about the phylogenic/bioinformatic strategy including some phylogenetic trees (supplemental figures 1 and 2); (ii) all data that were previously not shown (mass spectrometry data, in vivo respiratory assays) are now included in the manuscript as supplemental figures/tables.We hope that we have now significantly improved our manuscript so you'll find it suitable for publication in the special issue of Mitochondrion dedicated to "Plant Mitochondria Biology". R: Primary MS data are now given in Supplemental Table 3 for each polypeptide for which the score was > 60. (BLAST alignments, Evalues, etc.) are actually presented in the paper to support the inference that a particular E. gracilis protein is a true homolog of a given kinetoplastid protein. The most important conclusion of t...

show abstract

“…Its apparent molecular mass was determined to be 207 kD. For Arabidopsis, 14 different subunits were described, until now termed Cox I, Cox II, Cox III, Cox Vb, Cox Vc, Cox VIa, Cox VIb, Cox VIc, and Cox X1 to Cox X6 (Millar et al, 2004a). The Cox X1 to X6 subunits are plant specific.…”

Section: The Protein Complex Proteome Of Arabidopsis Mitochondriamentioning

confidence: 99%

“…The BN/SDS-PAGE analyses published to date allowed the identification of limited sets of proteins forming part of the mitochondrial proteome of potato (Solanum tuberosum;Jänsch et al, 1996 [16 proteins]; Bykova et al, 2003a [eight proteins]), Arabidopsis (Werhahn and Braun, 2002 [14 proteins]; Giegé et al, 2003 [26 proteins]), rice (Oryza sativa; Heazlewood et al, 2003b [57 proteins]; Millar et al, 2004b [18 proteins]), and Arum maculatum (Sunderhaus et al, 2010 [nine proteins]). Furthermore, 2D BN/SDS-PAGE was extensively used to systematically analyze subunits of individual protein complexes of plant mitochondria, like complex I (Heazlewood et al, 2003a;Millar et al, 2003;Sunderhaus et al, 2006;Meyer et al, 2007Meyer et al, , 2008Klodmann et al, 2010;Klodmann and Braun, 2011), complexes II and IV (Eubel et al, 2003;Millar et al, 2004a;Huang et al, 2010), complex III (Meyer et al, 2008), complex V (Heazlewood et al, 2003c;Meyer et al, 2008), the I+III 2 supercomplex (Peters et al, 2008), the formate dehydrogenase complex (Bykova et al, 2003b), and the TOM complex (Jänsch et al, 1998;Werhahn et al, 2001Werhahn et al, , 2003.…”

mentioning

confidence: 99%

Defining theProtein Complex Proteomeof Plant Mitochondria

et al. 2011

Self Cite

View full text Add to dashboard Cite

A classical approach, protein separation by two-dimensional blue native/sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was combined with tandem mass spectrometry and up-to-date computer technology to characterize the mitochondrial "protein complex proteome" of Arabidopsis (Arabidopsis thaliana) in so far unrivaled depth. We further developed the novel GelMap software package to annotate and evaluate two-dimensional blue native/sodium dodecyl sulfate gels. The software allows (1) annotation of proteins according to functional and structural correlations (e.g. subunits of a distinct protein complex), (2) assignment of comprehensive protein identification lists to individual gel spots, and thereby (3) selective display of protein complexes of low abundance. In total, 471 distinct proteins were identified by mass spectrometry, several of which form part of at least 35 different mitochondrial protein complexes. To our knowledge, numerous protein complexes were described for the first time (e.g. complexes including pentatricopeptide repeat proteins involved in nucleic acid metabolism). Discovery of further protein complexes within our data set is open to everybody via the public GelMap portal at www.gelmap.de/arabidopsis_mito.

show abstract

Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits

Cited by 177 publications

References 67 publications

Differential Impact of Environmental Stresses on the Pea Mitochondrial Proteome

Differential Impact of Environmental Stresses on the Pea Mitochondrial Proteome

The mitochondrial respiratory chain of the secondary green alga Euglena gracilis shares many additional subunits with parasitic Trypanosomatidae

Defining theProtein Complex Proteomeof Plant Mitochondria

Contact Info

Product

Resources

About