Publications [#355067] of Lucia C. Strader
search PubMed.Papers Published
- Korasick, DA; Chatterjee, S; Tonelli, M; Dashti, H; Lee, SG; Westfall, CS; Fulton, DB; Andreotti, AH; Amarasinghe, GK; Strader, LC; Jez, JM, Defining a two-pronged structural model for PB1 (Phox/Bem1p) domain interaction in plant auxin responses.,
The Journal of biological chemistry, vol. 290 no. 20
(May, 2015),
pp. 12868-12878 [doi] .
(last updated on 2026/01/18)Abstract:
Phox/Bem1p (PB1) domains are universal structural modules that use surfaces of different charge for protein-protein association. In plants, PB1-mediated interactions of auxin response factors (ARF) and auxin/indole 3-acetic acid inducible proteins regulate transcriptional events modulated by the phytohormone auxin. Here we investigate the thermodynamic and structural basis for Arabidopsis thaliana ARF7 PB1 domain self-interaction. Isothermal titration calorimetry and NMR experiments indicate that key residues on both the basic and acidic faces of the PB1 domain contribute to and organize coordinately to stabilize protein-protein interactions. Calorimetric analysis of ARF7PB1 site-directed mutants defines a two-pronged electrostatic interaction. The canonical PB1 interaction between a lysine and a cluster of acidic residues provides one prong with an arginine and a second cluster of acidic residues defining the other prong. Evolutionary conservation of this core recognition feature and other co-varying interface sequences allows for versatile PB1-mediated interactions in auxin signaling.