Structure Report for: 3WIO

Nakamura, H., Xue, Y.-L., Miyakawa, T., Hou, F., Qin, H.-M., Fukui, K., Shi, X., Ito, E., Ito, S., Park, S.-H., Miyauchi, Y., Asano, A., Totsuka, N., Ueda, T., Tanokura, M., Asami, T.

Title: Molecular mechanism of strigolactone perception by DWARF14
Nakamura H, Xue YL, Miyakawa T, Hou F, Qin HM, Fukui K, Shi X, Ito E, Ito S and Asami T <6 more author(s)> Nakamura H, Xue YL, Miyakawa T, Hou F, Qin HM, Fukui K, Shi X, Ito E, Ito S, Park SH, Miyauchi Y, Asano A, Totsuka N, Ueda T, Tanokura M, Asami T (- 6)
Ref: Nat Commun, 4:2613, 2013 : PubMed
Abstract


ESTHER: Nakamura_2013_Nat.Commun_4_2613
PubMedSearch: Nakamura 2013 Nat.Commun 4 2613
PubMedID: 24131983
Gene_locus related to this paper: orysj-Q10QA5
Inhibitor(s) related to this paper: Hydroxy-D-ring

Abstract

Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An alpha/beta-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.