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Title: Defining a Two-pronged Structural Model for PB1 (Phox/Bem1p) Domain Interaction in Plant Auxin Responses

Journal Article · · Journal of Biological Chemistry
 [1];  [2];  [3];  [3];  [1];  [1];  [4];  [4];  [2];  [1];  [1]
  1. Washington Univ., St. Louis, MO (United States)
  2. Washington Univ. School of Medicine, St. Louis, MO (United States)
  3. Univ. of Wisconsin, Madison, WI (United States)
  4. Iowa State Univ., Ames, IA (United States)

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. Furthermore, 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.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
National Institutes of Health (NIH); National Science Foundation (NSF); USDA, National Institute of Food and Agriculture (NIFA)
Grant/Contract Number:
P41GM103399; P41RR002301; S10RR02781; S10RR08438; S10RR023438; S10RR025062; S10RR029220; DMB-8415048; OIA-9977486; BIR-9214394; R00 GM089987-03; MOW-2010-05240; MOW-2014-01877; MCB-1157771
OSTI ID:
1351393
Journal Information:
Journal of Biological Chemistry, Vol. 290, Issue 20; ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular BiologyCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 26 works
Citation information provided by
Web of Science

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Cited By (6)

Regulation of auxin transcriptional responses journal April 2020
Evolutionary analyses of NIN-like proteins in plants and their roles in nitrate signaling journal June 2019
A genome‐wide association study approach to the identification of candidate genes underlying agronomic traits in alfalfa ( Medicago sativa L.) journal September 2019
Auxin response factors: Auxin response factors journal January 2016
A Review of Auxin Response Factors (ARFs) in Plants journal February 2016
Aux/IAA Gene Family in Plants: Molecular Structure, Regulation, and Function journal January 2018