Immunoaffinity purification of endogenous proteins from S. cerevisiae for post-translational modification and protein interaction analysis
| dc.contributor.author | Jaiswal, Deepika | |
| dc.contributor.author | Turniansky, Rashi | |
| dc.contributor.author | Green, Erin | |
| dc.date.accessioned | 2023-01-25T15:11:30Z | |
| dc.date.available | 2023-01-25T15:11:30Z | |
| dc.date.issued | 2021-11-19 | |
| dc.description.abstract | Protein regulation by post-translational modifications and protein-protein interactions is critical to controlling molecular pathways. Here, we describe an immunoaffinity purification approach in Saccharomyces cerevisiae. The protocol uses an endogenously-expressed epitope-tagged protein and can be applied to the identification of post-translational modifications or protein binding partners. The lysine methyltransferase Set5 is used as an example here to purify phosphorylated Set5 and identify phosphosites; however, this approach can be applied to a diverse set of proteins in yeast. | en_US |
| dc.description.sponsorship | The authors acknowledge members of the Green Lab for technical feedback and comments on the manuscript. We also thank James Moresco and John R. Yates III (Scripps Research Institute) for performing the mass spectrometry analysis associated with the original research published in Jaiswal et al. (2020). This work is funded by National Institutes of Health (NIH) grants R01GM124342 and R21AG064507 to E.M.G. | en_US |
| dc.description.uri | https://star-protocols.cell.com/protocols/1170 | en_US |
| dc.format.extent | 16 pages | en_US |
| dc.genre | journal articles | en_US |
| dc.identifier | doi:10.13016/m2ndos-otgr | |
| dc.identifier.citation | Jaiswal, Deepika, Rashi Turniansky and Erin M. Green. “Immunoaffinity purification of endogenous proteins from S. cerevisiae for post-translational modification and protein interaction analysis.” STAR Protocols 2, 100945 (December 17, 2021). https://doi.org/10.1016/j.xpro.2021.100945 | en_US |
| dc.identifier.uri | https://doi.org/10.1016/j.xpro.2021.100945 | |
| dc.identifier.uri | http://hdl.handle.net/11603/26706 | |
| dc.language.iso | en_US | en_US |
| dc.publisher | Cell Press | en_US |
| dc.relation.isAvailableAt | The University of Maryland, Baltimore County (UMBC) | |
| dc.relation.ispartof | UMBC Biological Sciences Department Collection | |
| dc.relation.ispartof | UMBC Faculty Collection | |
| dc.relation.ispartof | UMBC Student Collection | |
| dc.rights | This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author. | en_US |
| dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) | * |
| dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
| dc.title | Immunoaffinity purification of endogenous proteins from S. cerevisiae for post-translational modification and protein interaction analysis | en_US |
| dc.type | Text | en_US |
| dcterms.creator | https://orcid.org/0000-0002-6514-7535 | en_US |
| dcterms.creator | https://orcid.org/0000-0003-3923-6726 | en_US |