The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
An histidine covalent receptor and butenolide complex mediates strigolactone perception
Open accessAbstract
Strigolactone plant hormones control plant architecture and are key players in both symbiotic and parasitic interactions. They contain an ABC tricyclic lactone connected to a butenolide group, the D-ring. The DWARF14 (D14) strigolactone receptor belongs to the superfamily of α/β-hydrolases and is known to hydrolyze the bond between the ABC lactone and the D-ring. Here we characterize the binding and catalytic functions of RAMOSUS3 (RMS3), the pea (Pisum sativum) ortholog of rice (Oryza sativa) D14 strigolactone receptor. Using novel profluorescent probes with strigolactone-like bioactivity, we show that RMS3 acts as a single-turnover enzyme that explains its apparent low enzymatic rate. We further demonstrate the formation of a covalent RMS3/D-ring complex, essential for bioactivity, in which the D-ring is attached to Histidine 247 of the catalytic triad. These results reveal an undescribed mechanism of plant hormone reception where the receptor performs an irreversible enzymatic reaction to generate its own ligand.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Sheldrick, G. M. (2008) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 87,804
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
Crystal structure refinement with SHELXL
Sheldrick, G. M. (2015) · Acta Crystallographica Section C Structural Chemistry · doi:10.1107/s2053229614024218 · Cited by 43,982
Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., & Kumar, S. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr121 · Cited by 39,969
Floral dip: a simplified method forAgrobacterium‐mediated transformation ofArabidopsis thaliana
Clough, S. J., & Bent, A. F. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00343.x · Cited by 21,934
Protein structure prediction on the Web: a case study using the Phyre server
Kelley, L. A., & Sternberg, M. J. E. (2009) · Nature Protocols · doi:10.1038/nprot.2009.2 · Cited by 4,175
Strigolactone inhibition of shoot branching
Gomez-Roldan, V., Fermas, S., Brewer, P. B., Puech-Pagès, V., Dun, E. A., Pillot, J.-P., Letisse, F., Matusova, R., Danoun, S., Portais, J.-C., et al. (2008) · Nature · doi:10.1038/nature07271 · Cited by 2,281
Self-citationInhibition of shoot branching by new terpenoid plant hormones
Umehara, M., Hanada, A., Yoshida, S., Akiyama, K., Arite, T., Takeda-Kamiya, N., Magome, H., Kamiya, Y., Shirasu, K., Yoneyama, K., et al. (2008) · Nature · doi:10.1038/nature07272 · Cited by 2,105
Presenting your structures: the CCP 4 mg molecular-graphics software
McNicholas, S., Potterton, E., Wilson, K. S., & Noble, M. E. M. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911007281 · Cited by 1,308
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(2025) · doi:10.1016/j.molp.2025.09.021 · Cited by 7
Metadata
- Authors
- de Saint Germain, A., Clavé, G., Badet-Denisot, M.-A., Pillot, J.-P., Cornu, D., Le Caer, J.-P., Burger, M., Pelissier, F., Retailleau, P., Turnbull, C., Bonhomme, S., Chory, J., Rameau, C., & Boyer, F.-D.
- Venue
- Nature Chemical Biology
- Published
- 2016-08-01
- Volume
- 12
- Issue
- 10
- Pages
- 787-794
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2497317806
- Cited by
- 283
- References
- 52
- FWCI
- 37.41
- Type
- journal article
- Language
- en
- Open access
- green
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- de Saint Germain, A., Clavé, G., Badet-Denisot, M.-A., Pillot, J.-P., Cornu, D., Le Caer, J.-P., Burger, M., Pelissier, F., Retailleau, P., Turnbull, C., Bonhomme, S., Chory, J., Rameau, C., & Boyer, F.-D. (2016). An histidine covalent receptor and butenolide complex mediates strigolactone perception. Nature Chemical Biology. https://doi.org/10.1038/nchembio.2147
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