title: Defining a two-pronged structural model for PB1 (Phox/Bem1p) domain interaction in plant auxin responses.
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.
authors.affiliation: From the Department of Biology, Washington University, St. Louis, Missouri 63130.
authors.forename: David A
authors.initials: DA
authors.lastname: Korasick
authors.affiliation: Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: Srirupa
authors.initials: S
authors.lastname: Chatterjee
authors.affiliation: National Magnetics Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin 53706, and.
authors.forename: Marco
authors.initials: M
authors.lastname: Tonelli
authors.affiliation: National Magnetics Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, Wisconsin 53706, and.
authors.forename: Hesam
authors.initials: H
authors.lastname: Dashti
authors.affiliation: From the Department of Biology, Washington University, St. Louis, Missouri 63130.
authors.forename: Soon Goo
authors.initials: SG
authors.lastname: Lee
authors.affiliation: From the Department of Biology, Washington University, St. Louis, Missouri 63130.
authors.forename: Corey S
authors.initials: CS
authors.lastname: Westfall
authors.affiliation: Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011.
authors.forename: D Bruce
authors.initials: DB
authors.lastname: Fulton
authors.affiliation: Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa 50011.
authors.forename: Amy H
authors.initials: AH
authors.lastname: Andreotti
authors.affiliation: Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: Gaya K
authors.initials: GK
authors.lastname: Amarasinghe
authors.affiliation: From the Department of Biology, Washington University, St. Louis, Missouri 63130.
authors.forename: Lucia C
authors.initials: LC
authors.lastname: Strader
authors.affiliation: From the Department of Biology, Washington University, St. Louis, Missouri 63130, jjez@biology2.wustl.edu.
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Jez
mesh_terms: D017360:Arabidopsis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007210:Indoleacetic Acids; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C503425:ARF7 protein, Arabidopsis; D029681:Arabidopsis Proteins; D007210:Indoleacetic Acids; D014157:Transcription Factors
keywords: nuclear magnetic resonance (NMR); plant biochemistry; plant hormone; protein structure; protein-protein interaction
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