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Propiconazole Is A Specific And Accessible Brassinosteroid (Br) Biosynthesis Inhibitor For Arabidopsis And Maize., Burkhard Schulz, Thomas Hartwig, Claudia Corvalan, Norman Best, Joshua Budka, Sunghwa Choe
Propiconazole Is A Specific And Accessible Brassinosteroid (Br) Biosynthesis Inhibitor For Arabidopsis And Maize., Burkhard Schulz, Thomas Hartwig, Claudia Corvalan, Norman Best, Joshua Budka, Sunghwa Choe
Burkhard Schulz
Brassinosteroids (BRs) are steroidal hormones that play pivotal roles during plant development. In addition to the characterization of BR deficient mutants, specific BR biosynthesis inhibitors played an essential role in the elucidation of BR function in plants. However, high costs and limited availability of common BR biosynthetic inhibitors constrain their key advantage as a species-independent tool to investigate BR function. We studied propiconazole (Pcz) as an alternative to the BR inhibitor brassinazole (Brz). Arabidopsis seedlings treated with Pcz phenocopied BR biosynthetic mutants. The steady state mRNA levels of BR, but not gibberellic acid (GA), regulated genes increased proportional to the …
Ethylene Receptors Function As Components Of High-Molecular-Mass Protein Complexes In Arabidopsis, Yi-Feng Chen, Zhiyong Gao, Robert J. Kerriss Iii, Wuyi Wang, Brad M. Binder, G. Eric Schaller
Ethylene Receptors Function As Components Of High-Molecular-Mass Protein Complexes In Arabidopsis, Yi-Feng Chen, Zhiyong Gao, Robert J. Kerriss Iii, Wuyi Wang, Brad M. Binder, G. Eric Schaller
Brad M. Binder
The gaseous plant hormone ethylene is perceived in Arabidopsis thaliana by a five-member receptor family composed of ETR1, ERS1, ETR2, ERS2, and EIN4. Methodology/Principal Findings Gel-filtration analysis of ethylene receptors solubilized from Arabidopsis membranes demonstrates that the receptors exist as components of high-molecular-mass protein complexes. The ERS1 protein complex exhibits an ethylene-induced change in size consistent with ligand-mediated nucleation of protein-protein interactions. Deletion analysis supports the participation of multiple domains from ETR1 in formation of the protein complex, and also demonstrates that targeting to and retention of ETR1 at the endoplasmic reticulum only requires the first 147 amino acids of …