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.
Skip Nav Destination
Article navigation
August 2010
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article|
July 26 2010
Protein–protein interactions
Mike P. Williamson;
Mike P. Williamson
1
*Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, U.K.
1To whom correspondence should be addressed (email m.williamson@sheffield.ac.uk).
Search for other works by this author on:
Michael J. Sutcliffe
Michael J. Sutcliffe
†School of Chemical Engineering and Analytical Science, The Mill, University of Manchester, Manchester M13 9PL, U.K.
Search for other works by this author on:
Biochem Soc Trans (2010) 38 (4): 875–878.
Article history
Received:
January 20 2010
Citation
Mike P. Williamson, Michael J. Sutcliffe; Protein–protein interactions. Biochem Soc Trans 1 August 2010; 38 (4): 875–878. doi: https://doi.org/10.1042/BST0380875
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.