Journal
GENOME RESEARCH
Volume 23, Issue 4, Pages 736-746Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gr.148346.112
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Funding
- 21C Frontier Microbial Genomics and Application Center Program [MG-11-2008-09-004-00]
- 21C Frontier Functional Proteomics Project [FPR08A1-060]
- SRC/ERC Program [2011-0006426]
- National Research Foundation of Korea [2010-0022887]
- Ministry of Education, Science and Technology Republic of Korea
- National Research Foundation of Korea [2010-0022887] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The definition of protein protein interactions (PPIs) in the natural cellular context is essential for properly understanding various biological processes. So far, however, most large-scale PPI analyses have not been performed in the natural cellular context. Here, we describe the construction of a Saccharomyces cerevisiae fusion library in which each endogenous gene is C-terminally tagged with the N-terminal fragment of Venus (VN) for a genome-wide bimolecular fluorescence complementation assay, a powerful technique for identifying PPIs in living cells. We illustrate the utility of the VN fusion library by systematically analyzing the interactome of the small ubiquitin-related modifier (SUMO) and provide previously unavailable information on the subcellular localization, types, and protease dependence of SUMO interactions. Our data set is highly complementary to the existing data sets and represents a useful resource for expanding the understanding of the physiological roles of SUMO. In addition, the VN fusion library provides a useful research tool that makes it feasible to systematically analyze PPIs in the natural cellular context.
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