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Structural Mechanism of Abscisic Acid Binding and Signaling by Dimeric PYR1
Noriyuki Nishimura,1,*
Kenichi Hitomi,2,3,*
Andrew S. Arvai,2,*
Robert P. Rambo,3,*
Chiharu Hitomi,2
Sean R. Cutler,4
Julian I. Schroeder,1
Elizabeth D. Getzoff2,
Abstract:
The phytohormone abscisic acid (ABA) acts in seed dormancy,plant development, drought tolerance, and adaptive responsesto environmental stresses. Structural mechanisms mediating ABAreceptor recognition and signaling remain unknown but are essentialfor understanding and manipulating abiotic stress resistance.Here, we report structures of pyrabactin resistance 1 (PYR1),a prototypical PYR/PYR1-like (PYL)/regulatory component of ABAreceptor (RCAR) protein that functions in early ABA signaling.The crystallographic structure reveals an /β helix–gripfold and homodimeric assembly, verified in vivo by coimmunoprecipitation.ABA binding within a large internal cavity switches structuralmotifs distinguishing ABA-free "open-lid" from ABA-bound "closed-lid"conformations. Small-angle x-ray scattering suggests that ABAsignals by converting PYR1 to a more compact, symmetric closed-liddimer. Site-directed PYR1 mutants designed to disrupt hormonebinding lose ABA-triggered interactions with type 2C proteinphosphatase partners in planta.
1 Division of Biological Sciences, Cell and Developmental Biology Section, University of California at San Diego, La Jolla, CA 92093, USA. 2 Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. 3 Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. 4 Department of Botany and Plant Sciences, Center for Plant Cell Biology, University of California at Riverside, Riverside, CA 92521, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: edg{at}scripps.edu
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