Details
Original language | English |
---|---|
Title of host publication | Plant Mitochondria |
Subtitle of host publication | Methods and Protocols |
Editors | Olivier Van Aken, Allan G. Rasmusson |
Publisher | Humana Press |
Pages | 101-110 |
Number of pages | 10 |
ISBN (electronic) | 978-1-0716-1653-6 |
ISBN (print) | 978-1-0716-1652-9 |
Publication status | Published - 2022 |
Publication series
Name | Methods in Molecular Biology |
---|---|
Volume | 2363 |
ISSN (Print) | 1064-3745 |
ISSN (electronic) | 1940-6029 |
Abstract
Most molecular functions depend on defined associations of proteins. Protein-protein interactions may be transient or long-lasting; they may lead to labile assemblies or more stable particles termed protein complexes. Studying protein-protein interactions is of prime importance for understanding molecular functions in cells. The complexome profiling approach allows to systematically analyze protein assemblies of cells or subcellular compartments. It combines separation of intact protein fractions by blue native (BN) polyacrylamide gel electrophoresis (PAGE) and protein identification as well as quantification by mass spectrometry. Complexome profiling has been successfully applied to characterize mitochondrial fractions of plants. In a typical experiment, more than 1000 mitochondrial proteins are identified and assigned to defined protein assemblies. It allows discovering so far unknown protein complexes, studying assembly pathways of protein complexes and even characterizing labile super- and megacomplexes in the >10 mega-Dalton range. We here present a complexome profiling protocol for the straightforward definition of the protein complex inventory of mitochondria or other subcellular compartments from plants.
Keywords
- Arabidopsis thaliana, Blue native polyacrylamide gel electrophoresis, Complexome profiling, Mass spectrometry, Plant mitochondria, Respiration, Viscum album
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
Sustainable Development Goals
Cite this
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Plant Mitochondria: Methods and Protocols. ed. / Olivier Van Aken; Allan G. Rasmusson. Humana Press, 2022. p. 101-110 (Methods in Molecular Biology; Vol. 2363).
Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review
}
TY - CHAP
T1 - Complexome Profiling of Plant Mitochondrial Fractions
AU - Schröder, Lucie
AU - Eubel, Holger
AU - Braun, Hans-Peter
PY - 2022
Y1 - 2022
N2 - Most molecular functions depend on defined associations of proteins. Protein-protein interactions may be transient or long-lasting; they may lead to labile assemblies or more stable particles termed protein complexes. Studying protein-protein interactions is of prime importance for understanding molecular functions in cells. The complexome profiling approach allows to systematically analyze protein assemblies of cells or subcellular compartments. It combines separation of intact protein fractions by blue native (BN) polyacrylamide gel electrophoresis (PAGE) and protein identification as well as quantification by mass spectrometry. Complexome profiling has been successfully applied to characterize mitochondrial fractions of plants. In a typical experiment, more than 1000 mitochondrial proteins are identified and assigned to defined protein assemblies. It allows discovering so far unknown protein complexes, studying assembly pathways of protein complexes and even characterizing labile super- and megacomplexes in the >10 mega-Dalton range. We here present a complexome profiling protocol for the straightforward definition of the protein complex inventory of mitochondria or other subcellular compartments from plants.
AB - Most molecular functions depend on defined associations of proteins. Protein-protein interactions may be transient or long-lasting; they may lead to labile assemblies or more stable particles termed protein complexes. Studying protein-protein interactions is of prime importance for understanding molecular functions in cells. The complexome profiling approach allows to systematically analyze protein assemblies of cells or subcellular compartments. It combines separation of intact protein fractions by blue native (BN) polyacrylamide gel electrophoresis (PAGE) and protein identification as well as quantification by mass spectrometry. Complexome profiling has been successfully applied to characterize mitochondrial fractions of plants. In a typical experiment, more than 1000 mitochondrial proteins are identified and assigned to defined protein assemblies. It allows discovering so far unknown protein complexes, studying assembly pathways of protein complexes and even characterizing labile super- and megacomplexes in the >10 mega-Dalton range. We here present a complexome profiling protocol for the straightforward definition of the protein complex inventory of mitochondria or other subcellular compartments from plants.
KW - Arabidopsis thaliana
KW - Blue native polyacrylamide gel electrophoresis
KW - Complexome profiling
KW - Mass spectrometry
KW - Plant mitochondria
KW - Respiration
KW - Viscum album
UR - http://www.scopus.com/inward/record.url?scp=85115871509&partnerID=8YFLogxK
U2 - 10.1007/978-1-0716-1653-6_9
DO - 10.1007/978-1-0716-1653-6_9
M3 - Contribution to book/anthology
C2 - 34545489
SN - 978-1-0716-1652-9
T3 - Methods in Molecular Biology
SP - 101
EP - 110
BT - Plant Mitochondria
A2 - Van Aken, Olivier
A2 - Rasmusson, Allan G.
PB - Humana Press
ER -