Dark-grown 4-day-old Arabidopsis thaliana
seedling expressing dsRUB1 under the control
of the constitutive CaMV 35S promoter
(Bostick et al, 2004)
seedling expressing dsRUB1 under the control
of the constitutive CaMV 35S promoter
(Bostick et al, 2004)
General structure for a RING-HC domain showing spacing
between metal-binding residues
(Stone et al, 2005)
(Stone et al, 2005)
Auxin accelerates the degradation of IAA1:LUC
in Arabidopsis seedlings
(Zenser et al, 2001)
in Arabidopsis seedlings
(Zenser et al, 2001)
We are studying the functions of RUB1, RUB2, and RUB3 in Arabidopsis. Covalent attachment of the ubiquitin-like protein RUB (NEDD8 in mammals) to the cullin subunit of SCF complexes appears to regulate their E3 ubiquitin ligase activity. We are working to understand the role of the RUB proteins in plant growth and development, with a particular emphasis on regulation of the ethylene biosynthesis pathway.
We are examining the activity of another family of proteins containing RING and variant RING domains. These domains have been implicated in the E3 ubiquitin ligase activity of many proteins. We seek to identify putative proteins containing these domains, verify their ligase activity using in vitro ubiquitination assays, identify interacting partners, and characterize their function in vivo by studying the phenotypes of plants with mutations in RING-domain-containing proteins.
Auxin signal transduction requires the ubiquitin/proteasome pathway. We are interested in studying the degradation of the AUX/IAA family of transcriptional repressors as well as other components of auxin signaling pathways. We hope to characterize the regions required for recognition of the proteolytic targets, and to learn more about the ways in which auxin affects the rate of proteolysis of specific substrates.
The Callis lab is part of the Section of Molecular and Cellular Biology, within the College of Biological Sciences at UC Davis |
||