Studying Protein–Protein Interactions In Planta Using Advanced Fluorescence Microscopy

2017 ◽  
pp. 267-285 ◽  
Author(s):  
Marc Somssich ◽  
Rüdiger Simon
Keyword(s):  
Fluorescence Microscopy ◽  
Protein Interactions ◽  
In Planta ◽  
Protein Protein Interactions

scholarly journals Screening a cDNA Library for Protein–Protein Interactions Directly in Planta

2012 ◽  
Vol 24 (5) ◽  
pp. 1746-1759 ◽  
Author(s):  
Lan-Ying Lee ◽  
Fu-Hui Wu ◽  
Chen-Tran Hsu ◽  
Shu-Chen Shen ◽  
Hsuan-Yu Yeh ◽  
...  
Keyword(s):  
Cdna Library ◽  
Protein Interactions ◽  
In Planta ◽  
Protein Protein Interactions

scholarly journals Quantitative analysis of dynamic protein-protein interactions in planta by a floated-leaf luciferase complementation imaging (FLuCI) assay using binary Gateway vectors

2011 ◽  
Vol 67 (3) ◽  
pp. 542-553 ◽  
Author(s):  
Christian Gehl ◽  
David Kaufholdt ◽  
Domenica Hamisch ◽  
Rolf Bikker ◽  
Jörg Kudla ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Protein Interactions ◽  
In Planta ◽  
Protein Protein Interactions ◽  
Gateway Vectors

scholarly journals Screening for in planta protein-protein interactions combining bimolecular fluorescence complementation with flow cytometry

Plant Methods ◽  
2012 ◽  
Vol 8 (1) ◽  
pp. 25 ◽  
Author(s):  
Kenneth Berendzen ◽  
Maik Böhmer ◽  
Niklas Wallmeroth ◽  
Sébastien Peter ◽  
Marko Vesić ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Protein Interactions ◽  
Bimolecular Fluorescence Complementation ◽  
In Planta ◽  
Protein Protein Interactions ◽  
Fluorescence Complementation ◽  
Bimolecular Fluorescence

scholarly journals Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction

2019 ◽  
Vol 20 (9) ◽  
pp. 2096 ◽  
Author(s):  
Dmitry V. Arkhipov ◽  
Sergey N. Lomin ◽  
Yulia A. Myakushina ◽  
Ekaterina M. Savelieva ◽  
Dmitry I. Osolodkin ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Hot Spots ◽  
Protein Complexes ◽  
Structural Features ◽  
Signaling Proteins ◽  
In Planta ◽  
Protein Protein Interactions ◽  
Response Regulators ◽  
Protein Surfaces

The signaling of cytokinins (CKs), classical plant hormones, is based on the interaction of proteins that constitute the multistep phosphorelay system (MSP): catalytic receptors—sensor histidine kinases (HKs), phosphotransmitters (HPts), and transcription factors—response regulators (RRs). Any CK receptor was shown to interact in vivo with any of the studied HPts and vice versa. In addition, both of these proteins tend to form a homodimer or a heterodimeric complex with protein-paralog. Our study was aimed at explaining by molecular modeling the observed features of in planta protein–protein interactions, accompanying CK signaling. For this purpose, models of CK-signaling proteins’ structure from Arabidopsis and potato were built. The modeled interaction interfaces were formed by rather conserved areas of protein surfaces, complementary in hydrophobicity and electrostatic potential. Hot spots amino acids, determining specificity and strength of the interaction, were identified. Virtual phosphorylation of conserved Asp or His residues affected this complementation, increasing (Asp-P in HK) or decreasing (His-P in HPt) the affinity of interacting proteins. The HK–HPt and HPt–HPt interfaces overlapped, sharing some of the hot spots. MSP proteins from Arabidopsis and potato exhibited similar properties. The structural features of the modeled protein complexes were consistent with the experimental data.

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