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Bimolecular fluorescence complementation analysis system for in vivo detection of protein–protein interaction in Saccharomyces cerevisiae
Abstract
The bimolecular fluorescence complementation (BiFC) assay has been widely accepted for studying in vivo detection of protein–protein interactions in several organisms. To facilitate the application of the BiFC assay to yeast research, we have created a series of plasmids that allow single‐step, PCR‐based C‐ or N‐terminal tagging of yeast proteins with yellow fluorescent protein fragments for BiFC assay. By examination of several interacting proteins (Sis1–Sis1, Net1–Sir2, Cet1–Cet1 and Pho2–Pho4), we demonstrate that the BiFC assay can be used to reliably analyse the occurrence and subcellular localization of protein–protein interactions in living yeast cells. The sequences for the described plasmids were submitted to the GenBank under Accession Nos: EF210802, pFA6a‐VN‐His3MX6; EF210803, pFA6a‐VC‐His3MX6; EF210804, pFA6a‐VN‐TRP1; EF210807, pFA6a‐VC‐TRP1; EF210808, pFA6a‐VN‐kanMX6; EF210809, pFA6a‐VC‐kanMX6; EF210810, pFA6a‐His3MX6‐P GAL1‐VN; EF210805, pFA6a‐His3MX6‐P GAL1‐VC; EF210806, pFA6a‐TRP1‐P GAL1‐VN; EF210811, pFA6a‐TRP1‐P GAL1‐VC; EF210812, pFA6a‐kanMX6‐P GAL1‐VN; EF210813, pFA6a‐kanMX6‐P GAL1‐VC; EF521883, pFA6a‐His3MX6‐P CET1‐VN; EF521884, pFA6a‐His3MX6‐P CET1‐VC; EF521885, pFA6a‐TRP1‐P CET1‐VN; EF521886, pFA6a‐TRP1‐P CET1‐VC; EF521887, pFA6a‐kanMX6‐P CET1‐VN; EF521888, pFA6a‐kanMX6‐P CET1‐VC. Copyright © 2007 John Wiley & Sons, Ltd.
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Cites
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248 · cited 5×
“Considering the fact that cells expressing the C-terminally GFPtagged Cet1 show a normal growth pattern (Huh et al., 2003), it is unlikely that C-terminal protein tagging disturbed the cellular function of Cet1 and caused the failure of BiFC complex formation.”
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Cited by
Shai, N., Yifrach, E., van Roermund, C. W. T., Cohen, N., Bibi, C., IJlst, L., Cavellini, L., Meurisse, J., Schuster, R., Zada, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03957-8 · Cited by 320
Panchaud, N., Péli-Gulli, M.-P., & De Virgilio, C. (2013) · Science Signaling · doi:10.1126/scisignal.2004112 · Cited by 286
Ha, C. W., & Huh, W.-K. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq895 · Cited by 77
Self-citationCastro, I. G., Shortill, S. P., Dziurdzik, S. K., Cadou, A., Ganesan, S., Valenti, R., David, Y., Davey, M., Mattes, C., Thomas, F. B., et al. (2022) · eLife · doi:10.7554/elife.74602 · Cited by 60
Metadata
- Authors
- Sung, M., & Huh, W.
- Venue
- Yeast
- Publisher
- Wiley
- Published
- 2007-05-29
- Volume
- 24
- Issue
- 9
- Pages
- 767-775
- ISSN
- 0749-503X (ISSN-L)
- 1097-0061
- OpenAlex
- W2160360032
- Cited by
- 189
- References
- 1
- FWCI
- 4.60
- Type
- journal article
- Language
- en
- Open access
- closed
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