Development and application of proteomics technologies in Saccharomyces cerevisiae

Kolkman, Annemieke; Slijper, Monique; Heck, Albert J. R.

doi:10.1016/j.tibtech.2005.09.004

Cited by 47 publications

(27 citation statements)

References 67 publications

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“…Using a proteomic approach, we described the differential protein profile of control and murine macrophages interacting with live and heat-inactivated C. albicans cells and a pro-and antiinflammatory effect was showed, respectively [17,18]. 2D-Difference Gel Electrophoresis (2D-DIGE) [19] is a powerful analytical tool within the field of proteomics, allowing not only the relative quantitation of protein spot intensity across carefully matched gels, but also for detecting posttranslational modifications of the protein [20]. Because gel-based techniques have a bias toward abundant proteins, proteins in lower quantity are not often detected in the 2-DE analysis of total cellular proteins due to the complexity of these samples.…”

Section: Introductionmentioning

confidence: 99%

Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus

Reales-Calderón

Martínez-Solano

Martínez-Gomáriz

et al. 2012

Journal of Proteomics

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Section: Introductionmentioning

confidence: 99%

Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus

Reales-Calderón

Martínez-Solano

Martínez-Gomáriz

et al. 2012

Journal of Proteomics

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“…First, we focused on the changes of the mitochondrial proteome during anaerobiosis by employing 14 N/ 15 N metabolic labeling [6,23,24] to aerobic and anaerobic steady-state chemostat cultures. Chemostat cultivation was used as it enables the accurate manipulation of individual culture parameters (e.g.…”

Section: Introductionmentioning

confidence: 99%

A three‐way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions

et al. 2009

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To investigate the effect of anaerobiosis on the Saccharomyces cerevisiae mitochondrial proteome and the formation of respiratory chain and other protein complexes, we analyzed mitochondrial protein extracts that were enriched from lysates of aerobic and anaerobic steady-state chemostat cultures. We chose an innovative approach in which native mitochondrial membrane protein complexes were separated by 1-D blue native PAGE, which was combined with quantitative analysis of each complex subunit using stable isotope labeling. LC-FT(ICR)-MS/MS analysis was applied to identify and quantify the mitochondrial proteins. In addition, to establish if changes in mitochondrial complex composition occurred under anaerobiosis, we investigated the 1-D blue native PAGE protein migration patterns by Pearson correlation analysis. Surprisingly, we discovered that under anaerobic conditions, where the yeast respiratory chain is not active, the respiratory chain supercomplexes, such as complex V dimer, complex (III) 2 (IV) 2 and complex (III) 2 (IV) were still present, although at reduced levels. Pearson correlation analysis showed that the composition of the mitochondrial complexes was unchanged under aerobic or anaerobic conditions, with the exception of complex II. In addition, this latter approach allowed screening for possible novel complex interaction partners, since for example protein Aim38p, with a yet unknown function, was identified as a possible component of respiratory chain complex IV.

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“…Second, a variety of genetic tools can be used to retard the destruction of newly ubiquitinated substrates, including proteasomal protease mutants and protease-resistant variants of ubiquitin. 91 In fact, Gpa1 represents the first example of direct identification of an in vivo ubiquitination site of any protein using mass spectrometry. This crucial information allowed the rational design of a mutant form of Gpa1 that does not undergo ubiquitination.…”

Section: Ubiquitination and Destruction Of Heterotrimeric G-protein Smentioning

confidence: 99%

Regulation of G Protein and Mitogen-Activated Protein Kinase Signaling by Ubiquitination

Wang

Dohlman

2006

Circulation Research

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Abstract-Guanine nucleotide binding proteins (G proteins) and mitogen-activated protein kinases are highly conserved signaling molecules engaged in a wide variety of cellular processes. The strength and duration of signaling mediated by G proteins and mitogen-activated protein kinases are well known to be regulated via phosphorylation of pathway components. Over the past few years, it has become evident that many of the same signaling proteins also undergo ubiquitination, a posttranslational modification that typically leads to protein degradation. Consequently the strength and duration of signaling can also be modulated by regulating the abundance of signaling proteins. This article describes G protein-and mitogen-activated protein kinase-mediated signaling pathways that are known to be regulated by ubiquitination. The focus is on studies performed in the budding yeast Saccharomyces cerevisiae, as many principles governing this new regulatory mechanism were initially discovered in this model organism. Similar mechanisms uncovered in other model systems are also briefly discussed to illustrate the importance and universality of signaling regulation by ubiquitination.

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Development and application of proteomics technologies in Saccharomyces cerevisiae

Cited by 47 publications

References 67 publications

Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus

Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus

A three‐way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions

Regulation of G Protein and Mitogen-Activated Protein Kinase Signaling by Ubiquitination

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