Katia Schütze

TL;DR: The implementation of a bimolecular fluorescence complementation technique for visualization of protein-protein interactions in plant cells revealed a remarkable signal fluorescence intensity of interacting protein complexes as well as a high reproducibility and technical simplicity of the method in different plant systems.

TL;DR: It is demonstrated that AtbZIP10 is a positive mediator of the uncontrolled cell death observed in lsd1 mutants, and likely functions as a cellular hub, where its interaction with LSD1 and additional, as yet unidentified, proteins contributes significantly to plant oxidative stress responses.

TL;DR: Dimmerisation studies making use of yeast and Arabidopsis protoplast‐based two‐hybrid systems, as well as bimolecular fluorescence complementation studies, reveal that AtbZIP53 does not preferentially form dimers with group‐S bZIPs but strongly interacts with members of group‐C.

TL;DR: Heterodimerization and expression data provide a basic framework to further determine the functional impact of the C/S1 network in regulating the plant energy balance and nutrient allocation.

TL;DR: A bimolecular fluorescence complementation (BiFC) technique for visualization of protein-protein interactions in plant cells, based on the formation of a fluorescent complex by two non-fluorescent fragments of the yellow fluorescent protein (YFP).