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Bimolecular Fluorescence Complementation as a Tool to Study Specific Dynamic Interactions Between Proteins in Fission Yeast.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2025; Vol. 2862, pp. 103-120. - Publication Year :
- 2025
-
Abstract
- Bimolecular fluorescence complementation (BiFC) is a technique that enables real-time observation within living cells of the interaction between two proteins forming a complex, determining the location where such interaction occurs within the cell, and even the association and dissociation cycles in response to physiological cues. Here, we describe in detail the use of bimolecular fluorescence complementation to visualize the assembly and disassembly of cohesin over the fission yeast cell cycle.<br /> (© 2025. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
- Subjects :
- Schizosaccharomyces pombe Proteins metabolism
Schizosaccharomyces pombe Proteins genetics
Microscopy, Fluorescence methods
Cohesins
Chromosomal Proteins, Non-Histone metabolism
Cell Cycle
Protein Interaction Mapping methods
Protein Binding
Schizosaccharomyces metabolism
Schizosaccharomyces genetics
Cell Cycle Proteins metabolism
Cell Cycle Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 2862
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 39527196
- Full Text :
- https://doi.org/10.1007/978-1-0716-4168-2_8