The proteome of Saccharomyces cerevisiae mitochondria

Sickmann, Albert; Reinders, Jörg; Wagner, Yvonne; Joppich, Cornelia; Zahedi, René P.; Meyer, Helmut E.; Schönfisch, Birgit; Perschil, Inge; Chacińska, Agnieszka; Guiard, Bernard; Rehling, Peter; Pfanner, Nikolaus; Meisinger, Chris

doi:10.1073/pnas.2135385100

Cited by 816 publications

(701 citation statements)

References 52 publications

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“…This number is essentially in accordance with the respective transcriptome data (see below). A large set of unclassified proteins was also found in recent plant, human, and yeast mitochondrial proteome analyses [28][29][30] and interpreted as an indication for a putative wealth of as yet undiscovered mitochondrial functions. By analogy, presence of a major set of proteins with unknown functions in pollen may hint at as yet unidentified cellular processes, of which some might be specific for the male gametophyte.…”

Section: Functional Categoriesmentioning

confidence: 86%

A reference map of the Arabidopsis thaliana mature pollen proteome

Noir

Bräutigam

Colby

et al. 2005

Biochemical and Biophysical Research Communications

134

145

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The male gametophyte (or pollen) plays an obligatory role during sexual reproduction of higher plants. The extremely reduced complexity of this organ renders pollen a valuable experimental system for studying fundamental aspects of plant biology such as cell fate determination, cell-cell interactions, cell polarity, and tip-growth. Here, we present the first reference map of the mature pollen proteome of the dicotyledonous model plant species, Arabidopsis thaliana. Based on two-dimensional gel electrophoresis, matrix-assisted laser desorption/ionization time-of-flight, and electrospray quadrupole time-of-flight mass spectrometry, we reproducibly identified 121 different proteins in 145 individual spots. The presence, subcellular localization, and functional classification of the identified proteins are discussed in relation to the pollen transcriptome and the full protein complement encoded by the nuclear Arabidopsis genome. Ó 2005 Elsevier Inc. All rights reserved.Keywords: Arabidopsis thaliana; Male gametophyte; Mass spectrometry; Mature pollen; Proteome; Two-dimensional gel electrophoresis In higher plants, development of the male gametophyte is a well-programmed and elaborate process. Male sporogenesis begins with the division of a diploid sporophytic cell giving rise to the anther wall of the stamen and the sporogenic cells. The latter cells then undergo several mitoses to differentiate into pollen mother cells. Subsequently, each diploid pollen mother cell forms a tetrad of haploid microspores via a round of DNA replication followed by two consecutive meiotic divisions. Each uninucleate microspore then undergoes an asymmetric mitotic division forming a large vegetative cell and a smaller generative cell (i.e., the bicellular pollen stage). In Arabidopsis, the generative cell undergoes another mitotic division giving rise to two sperm cells (i.e., the tricellular pollen stage). Following pollination, the vegetative cell controls the further development of the mature pollen grain and growth of the pollen tube into the style until both sperm cell nuclei are delivered to the embryo sac in the ovule, where they participate in double fertilization [1,2].The last two decades have been marked by increasing efforts to decipher the genetic and molecular basis of pollen development and functions [reviewed in 1,3,4]. In the model plant Arabidopsis thaliana, the extremely reduced, tricellular male gametophyte constitutes an ideal experimental system for analyses of important biological processes in higher plant reproduction. In addition, it represents a very useful model for studying fundamental aspects of plant biology such as cell fate determination, cell-cell interactions, cell polarity, and tip-growth [5][6][7].The availability of the full genome sequence of Arabidopsis [8] has made genome-wide, microarray-based analyses of the male gametophyte transcriptome of this model plant possible [9][10][11][12]. 13,977 male gametophyte-expressed mRNAs were recently identified using the ATH1 Genome Array, which cover...

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Section: Functional Categoriesmentioning

confidence: 86%

A reference map of the Arabidopsis thaliana mature pollen proteome

Noir

Bräutigam

Colby

et al. 2005

Biochemical and Biophysical Research Communications

134

145

View full text Add to dashboard Cite

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“…(b) Many of these fluorescein-labeled proteins exhibit multiple isoforms (labeled with letters) with slight differences in apparent molecular weights and isoelectric points. Multiple isoforms are common in two-dimensional analyses of yeast cellular proteins [24][25][26][27][28]. (c) Many of the same proteins were found to contain disulfide bonds in oleate-shifted cells (gels not shown).…”

Section: Assays For Disulfide Bondsmentioning

confidence: 99%

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Minard

Carroll

Weintraub

et al. 2007

Free Radical Biology and Medicine

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A yeast mutant lacking the two major cytosolic sources of NADPH, glucose-6-phosphate dehydrogenase (Zwf1p) and NADP + -specific isocitrate dehydrogenase (Idp2p), has been demonstrated to lose viability when shifted to medium with acetate or oleate as the carbon source. This loss in viability was found to correlate with an accumulation of endogenous oxidative byproducts of respiration and peroxisomal β-oxidation. To assess effects on cellular protein of endogenous versus exogenous oxidative stress, a proteomics approach was used to compare disulfide bondcontaining proteins in the idp2Δzwf1Δ strain following shifts to acetate and oleate media with those in the parental strain following similar shifts to media containing hydrogen peroxide. Among prominent disulfide bond-containing proteins were several with known antioxidant functions. These and several other proteins were detected as multiple electrophoretic isoforms, with some isoforms containing disulfide bonds under all conditions and other isoforms exhibiting a redox-sensitive content of disulfide bonds, i.e., in the idp2Δzwf1Δ strain and in the hydrogen peroxide-challenged parental strain. The disulfide bond content of some isoforms of these proteins was also elevated in the parental strain grown on glucose, possibly suggesting a redirection of NADPH reducing equivalents to support rapid growth. Further examination of protein carbonylation in the idp2Δzwf1Δ strain shifted to oleate medium also led to identification of common and unique protein targets of endogenous oxidative stress.

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“…While 2-D PAGE has been employed toward an inventory of the mitochondrial proteome [7,11,[15][16][17][18][19], mitochondria contain many membrane-bound and very basic proteins that are quite difficult to be analyzed by 2-D PAGE [7,14]. Consequently, considerable efforts have been devoted to the application of various LC techniques in single or multidimensional separation format prior to MS detection for the analysis of mitochondrial proteins [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, considerable efforts have been devoted to the application of various LC techniques in single or multidimensional separation format prior to MS detection for the analysis of mitochondrial proteins [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31]. In particular, the peptide-based shotgun proteomic studies fully exploit the resolution and sensitivity achievable with multidimensional LC-MS or SDS-PAGE/LC-MS approaches, allowing many additional mitochondrial proteins to be identified.…”

Section: Introductionmentioning

confidence: 99%

Application of capillary isotachophoresis‐based multidimensional separations coupled with electrospray ionization‐tandem mass spectrometry for characterization of mouse brain mitochondrial proteome

et al. 2008

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By employing a capillary ITP (CITP)/CZE-based proteomic technology, a total of 1795 distinct mouse Swiss-Prot protein entries (or 1705 nonredundant proteins) are identified from synaptic mitochondria isolated from mouse brain. The ultrahigh resolving power of CITP/CZE is evidenced by the large number of distinct peptide identifications measured from each CITP fraction together with the low peptide fraction overlapping among identified peptides. The degree of peptide overlapping among CITP fractions is even lower than that achieved using combined CIEF/nano-RP LC separations for the analysis of the same mitochondrial sample. When evaluating the protein sequence coverage by the number of distinct peptides mapping to each mitochondrial protein identification, CITP/CZE similarly achieves superior performance with 1041 proteins (58%) having 3 or more distinct peptides, 233 (13%) having 2 distinct peptides, and 521 (29%) having a single distinct peptide. The reproducibility of protein identifications is found to be around 86% by comparing proteins identified from repeated runs of the same mitochondrial sample. The analysis of the mouse mitochondrial proteome by two CITP/CZE runs results in the detection of 2095 distinct mouse Swiss-Prot protein entries (or 1992 nonredundant proteins), corresponding to 59% coverage of the updated Maestro mitochondrial reference set. The collective analysis from combined CITP/CZE and CIEF-based proteomic studies yields the identification of 2191 distinct mitochondrial protein entries (or 2082 nonredundant proteins), corresponding to 76% coverage of the MitoP2-database reference set.

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The proteome of Saccharomyces cerevisiae mitochondria

Cited by 816 publications

References 52 publications

A reference map of the Arabidopsis thaliana mature pollen proteome

A reference map of the Arabidopsis thaliana mature pollen proteome

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Application of capillary isotachophoresis‐based multidimensional separations coupled with electrospray ionization‐tandem mass spectrometry for characterization of mouse brain mitochondrial proteome

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