Author
Listed:
- Hidemitsu Nakamura
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- You-Lin Xue
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Takuya Miyakawa
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Feng Hou
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Hui-Min Qin
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Kosuke Fukui
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Xuan Shi
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Emi Ito
(Graduate School of Science, The University of Tokyo)
- Shinsaku Ito
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Seung-Hyun Park
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Yumiko Miyauchi
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Atsuko Asano
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Naoya Totsuka
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Takashi Ueda
(Graduate School of Science, The University of Tokyo)
- Masaru Tanokura
(Graduate School of Agricultural and Life Sciences, The University of Tokyo)
- Tadao Asami
(Graduate School of Agricultural and Life Sciences, The University of Tokyo
JST, CREST, 4-1-8 Honcho, Kawaguchi)
Abstract
Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An α/β-hydrolase protein, DWARF14 (D14), has been recognized to be an essential component of plant SL signalling, although its precise function remains unknown. Here we present the SL-dependent interaction of D14 with a gibberellin signalling repressor SLR1 and a possible mechanism of phytohormone perception in D14-mediated SL signalling. D14 functions as a cleavage enzyme of SLs, and the cleavage reaction induces the interaction with SLR1. The crystal structure of D14 shows that 5-hydroxy-3-methylbutenolide (D-OH), which is a reaction product of SLs, is trapped in the catalytic cavity of D14 to form an altered surface. The D14 residues recognizing D-OH are critical for the SL-dependent D14−SLR1 interaction. These results provide new insight into crosstalk between gibberellin and SL signalling pathways.
Suggested Citation
Hidemitsu Nakamura & You-Lin Xue & Takuya Miyakawa & Feng Hou & Hui-Min Qin & Kosuke Fukui & Xuan Shi & Emi Ito & Shinsaku Ito & Seung-Hyun Park & Yumiko Miyauchi & Atsuko Asano & Naoya Totsuka & Taka, 2013.
"Molecular mechanism of strigolactone perception by DWARF14,"
Nature Communications, Nature, vol. 4(1), pages 1-10, December.
Handle:
RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3613
DOI: 10.1038/ncomms3613
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