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Protein–protein interactions
- Source :
- Biochemical Society Transactions. 38:875-878
- Publication Year :
- 2010
- Publisher :
- Portland Press Ltd., 2010.
-
Abstract
- In the present article, we describe the two standard high-throughput methods for identification of protein complexes: two-hybrid screens and TAP (tandem affinity purification) tagging. These methods have been used to characterize the interactome of Saccharomyces cerevisiae, showing that the majority of proteins are part of complexes, and that complexes typically consist of a core to which are bound ‘party’ and ‘dater’ proteins. Complexes typically are merely the sum of their parts. A particularly interesting type of complex is the metabolon, containing enzymes within the same metabolic pathway. There is reasonably good evidence that metabolons exist, but they have not been detected using high-thoughput assays, possibly because of their fragility.
- Subjects :
- chemistry.chemical_classification
Tandem affinity purification
Saccharomyces cerevisiae Proteins
biology
Chemistry
Saccharomyces cerevisiae
Proteins
biology.organism_classification
Models, Biological
Biochemistry
Interactome
Yeast
High-Throughput Screening Assays
Protein–protein interaction
Metabolic pathway
Enzyme
Two-Hybrid System Techniques
Protein Interaction Mapping
Animals
Humans
Metabolon
Protein Binding
Subjects
Details
- ISSN :
- 14708752 and 03005127
- Volume :
- 38
- Database :
- OpenAIRE
- Journal :
- Biochemical Society Transactions
- Accession number :
- edsair.doi.dedup.....eb5425da813a18fa6f06afe0a00662fd