Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-01

AUTHORS

Yuen Ho, Albrecht Gruhler, Adrian Heilbut, Gary D. Bader, Lynda Moore, Sally-Lin Adams, Anna Millar, Paul Taylor, Keiryn Bennett, Kelly Boutilier, Lingyun Yang, Cheryl Wolting, Ian Donaldson, Søren Schandorff, Juanita Shewnarane, Mai Vo, Joanne Taggart, Marilyn Goudreault, Brenda Muskat, Cris Alfarano, Danielle Dewar, Zhen Lin, Katerina Michalickova, Andrew R. Willems, Holly Sassi, Peter A. Nielsen, Karina J. Rasmussen, Jens R. Andersen, Lene E. Johansen, Lykke H. Hansen, Hans Jespersen, Alexandre Podtelejnikov, Eva Nielsen, Janne Crawford, Vibeke Poulsen, Birgitte D. Sørensen, Jesper Matthiesen, Ronald C. Hendrickson, Frank Gleeson, Tony Pawson, Michael F. Moran, Daniel Durocher, Matthias Mann, Christopher W. V. Hogue, Daniel Figeys, Mike Tyers

ABSTRACT

The recent abundance of genome sequence data has brought an urgent need for systematic proteomics to decipher the encoded protein networks that dictate cellular function. To date, generation of large-scale protein-protein interaction maps has relied on the yeast two-hybrid system, which detects binary interactions through activation of reporter gene expression. With the advent of ultrasensitive mass spectrometric protein identification methods, it is feasible to identify directly protein complexes on a proteome-wide scale. Here we report, using the budding yeast Saccharomyces cerevisiae as a test case, an example of this approach, which we term high-throughput mass spectrometric protein complex identification (HMS-PCI). Beginning with 10% of predicted yeast proteins as baits, we detected 3,617 associated proteins covering 25% of the yeast proteome. Numerous protein complexes were identified, including many new interactions in various signalling pathways and in the DNA damage response. Comparison of the HMS-PCI data set with interactions reported in the literature revealed an average threefold higher success rate in detection of known complexes compared with large-scale two-hybrid studies. Given the high degree of connectivity observed in this study, even partial HMS-PCI coverage of complex proteomes, including that of humans, should allow comprehensive identification of cellular networks. More... »

PAGES

180

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/415180a

DOI

http://dx.doi.org/10.1038/415180a

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005267371

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11805837


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