Chris Meisinger

ORCID: 0000-0002-8326-3548
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • RNA and protein synthesis mechanisms
  • Metabolism and Genetic Disorders
  • RNA modifications and cancer
  • Fibroblast Growth Factor Research
  • Photosynthetic Processes and Mechanisms
  • Ubiquitin and proteasome pathways
  • Trypanosoma species research and implications
  • Endoplasmic Reticulum Stress and Disease
  • Autophagy in Disease and Therapy
  • RNA Research and Splicing
  • Advanced Proteomics Techniques and Applications
  • Heat shock proteins research
  • Fungal and yeast genetics research
  • Metabolomics and Mass Spectrometry Studies
  • Proteoglycans and glycosaminoglycans research
  • Adipose Tissue and Metabolism
  • Lipid metabolism and biosynthesis
  • Nerve injury and regeneration
  • Neuroscience of respiration and sleep
  • Biochemical and Molecular Research
  • Cell death mechanisms and regulation
  • Genetics and Neurodevelopmental Disorders
  • Mass Spectrometry Techniques and Applications

University of Freiburg
2016-2025

Biologie Labor
2014

Institute of Molecular Biotechnology
2014

Czech Academy of Sciences, Biology Centre
2011-2012

University of Bern
2011-2012

Institute of Molecular Medicine
2006

University of Würzburg
2006

Ruhr University Bochum
2003

We performed a comprehensive approach to determine the proteome of Saccharomyces cerevisiae mitochondria. The proteins highly pure yeast mitochondria were separated by several independent methods and analyzed tandem MS. From >20 million MS spectra, 750 different identified, indicating an involvement in numerous cellular processes. All known components oxidative phosphorylation machinery, tricarboxylic acid cycle, stable mitochondria-encoded found. Based on mitochondrial described...

10.1073/pnas.2135385100 article EN Proceedings of the National Academy of Sciences 2003-10-23

Proteomic analyses of different subcellular compartments, so-called organellar proteomics, facilitate the understanding cellular functions on a molecular level. In this work, various orthogonal multidimensional separation techniques both protein and peptide level are compared with regard to number identified proteins as well classes accessible by respective methodology. The most complete overview was achieved combination such shown analysis yeast mitochondrial proteome. A total 851 (PROMITO...

10.1021/pr050477f article EN Journal of Proteome Research 2006-06-06

The presequence translocase of the inner mitochondrial membrane (TIM23 complex) operates at a central junction protein import. It accepts preproteins from outer TOM complex and directs them to insertion or, in cooperation with translocase-associated motor (PAM), matrix. Little is known how TIM23 coordinates these tasks. We have identified Tim21 (YGR033c) that interacts complex. specific for form cooperates promotes insertion. Protein translocation into matrix requires switch Tim21-free, PAM...

10.1016/j.cell.2005.01.011 article EN cc-by-nc-nd Cell 2005-03-01

Abstract Early dissemination, metastasis and therapy resistance are central hallmarks of aggressive cancer types the leading cause cancer-associated deaths. The EMT-inducing transcriptional repressor ZEB1 is a crucial stimulator these processes, particularly by coupling activation cellular motility with stemness survival properties. expression associated behaviour in many tumour types, but potent effects cannot be solely explained its proven function as epithelial genes. Here we describe...

10.1038/ncomms10498 article EN cc-by Nature Communications 2016-02-15

The mitochondrial inner membrane contains a large protein complex that functions in organization and formation of contact sites. was variably named the site complex, organizing system, structure, or Mitofilin/Fcj1 complex. To facilitate future studies, we propose to unify nomenclature term "mitochondrial cristae system" its subunits Mic10 Mic60.

10.1083/jcb.201401006 article EN cc-by-nc-sa The Journal of Cell Biology 2014-03-31

The preprotein translocase of the outer mitochondrial membrane (TOM complex) contains one essential subunit, channel Tom40. assembly pathway precursor Tom40 involves TOM complex and sorting machinery (SAM with non-essential subunit Mas37. We have identified Sam50, second protein membrane. Sam50 a β-barrel domain conserved from bacteria to man is SAM complex. Yeast mutants are defective in pathways abundant porin, while import matrix proteins not affected. Thus an essential, protein. large...

10.1074/jbc.c300442200 article EN cc-by Journal of Biological Chemistry 2003-11-26

The biogenesis of mitochondrial outer membrane proteins involves the general translocase (TOM complex) and sorting assembly machinery (SAM complex). two known subunits SAM complex, Mas37 Sam50, are required for abundant porin Tom40. We have identified an unexpected subunit Mdm10, which is involved in maintenance morphology. Mitochondria lacking Mdm10 selectively impaired final steps pathway Tom40, including association Tom40 with receptor Tom22 small Tom proteins, while not affected. Yeast...

10.1016/j.devcel.2004.06.003 article EN cc-by-nc-nd Developmental Cell 2004-07-01

Often preparations of isolated organelles contain other, unwanted, cellular components. For biochemical experiments to determine the localization newly identified proteins, or whole set proteins (or proteome) from a desired organelle, these unwanted components often confuse resulting data. types studies, it is crucial have highly pure fractions organelle. Here we describe protocol for purification mitochondria Saccharomyces cerevisiae cells devoid contamination other compartments.

10.1385/1-59259-958-3:033 article EN Humana Press eBooks 2005-08-23

Mitochondria consist of four compartments-outer membrane, intermembrane space, inner and matrix--with crucial but distinct functions for numerous cellular processes. A comprehensive characterization the proteome an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, yeast Saccharomyces cerevisiae, to determine highly purified outer membranes. obtained coverage approximately 85% based on known membrane proteins. The represents rich source...

10.1091/mbc.e05-08-0740 article EN Molecular Biology of the Cell 2006-01-12
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