Home LiteratureArticle Details
PMID: 21666666 Published · epublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Structural insight into brassinosteroid perception by BRI1.

Nature ·Vol. 474 ·No. 7352 ·2011-06-12 ·Pages 472-6

She J, Han Z, Kim TW, Wang J, Cheng W, Chang J, Shi S, Wang J, Yang M, Wang ZY, Chai J

Abstract

Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation.

MeSH Terms
Arabidopsis/chemistry,metabolism Arabidopsis Proteins/chemistry,metabolism Binding Sites Brassinosteroids Cholestanols/chemistry,metabolism Crystallography, X-Ray Enzyme Activation Hydrophobic and Hydrophilic Interactions Models, Molecular Protein Binding Protein Folding Protein Kinases/chemistry,metabolism Protein Structure, Tertiary Steroids, Heterocyclic/chemistry,metabolism Structure-Activity Relationship Substrate Specificity
Chemicals
Arabidopsis Proteins Brassinosteroids Cholestanols Steroids, Heterocyclic Protein Kinases BRI1 protein, Arabidopsis brassinolide
Authors & Affiliations
11 authors, click to expand affiliations / ORCID
She Ji
Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University, Beijing 100084, China.
Han Zhifu
Kim Tae-Wuk
Wang Jinjing
Cheng Wei
Chang Junbiao
Shi Shuai
Wang Jiawei
Yang Maojun
Wang Zhi-Yong
Chai Jijie
References (34)
34 references, click to expand
  1. Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor.
    Nature. 2010 Nov 18;468(7322):400-5 PMID: 20927106
  2. A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction.
    Cell. 1997 Sep 5;90(5):929-38 PMID: 9298904
  3. Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteroid insensitive 1 receptor oligomerization.
    Biophys J. 2008 Feb 1;94(3):1052-62 PMID: 17905839
  4. BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.
    Cell. 2002 Jul 26;110(2):203-12 PMID: 12150928
  5. Autoregulation and homodimerization are involved in the activation of the plant steroid receptor BRI1.
    Dev Cell. 2005 Jun;8(6):855-65 PMID: 15935775
  6. The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense.
    Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):10124-8 PMID: 12904578
  7. Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1.
    Science. 2000 Jun 30;288(5475):2360-3 PMID: 10875920
  8. Coot: model-building tools for molecular graphics.
    Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32 PMID: 15572765
  9. Comparative analysis of the receptor-like kinase family in Arabidopsis and rice.
    Plant Cell. 2004 May;16(5):1220-34 PMID: 15105442
  10. Structural basis of toll-like receptor 3 signaling with double-stranded RNA.
    Science. 2008 Apr 18;320(5874):379-81 PMID: 18420935
  11. Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase.
    Science. 2002 Feb 15;295(5558):1299-301 PMID: 11847343
  12. Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.
    Nature. 2005 Jan 13;433(7022):167-71 PMID: 15650741
  13. Phaser crystallographic software.
    J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674 PMID: 19461840
  14. Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.
    Plant Cell. 2005 Jun;17(6):1685-703 PMID: 15894717
  15. Integration of brassinosteroid signal transduction with the transcription network for plant growth regulation in Arabidopsis.
    Dev Cell. 2010 Nov 16;19(5):765-77 PMID: 21074725
  16. Plant biology: Signal advance for abscisic acid.
    Nature. 2009 Dec 3;462(7273):575-6 PMID: 19956245
  17. Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1).
    Plant Cell. 2004 Dec;16(12):3216-29 PMID: 15548744
  18. Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane.
    Science. 2006 Aug 25;313(5790):1118-22 PMID: 16857903
  19. Molecular mechanisms of steroid hormone signaling in plants.
    Annu Rev Cell Dev Biol. 2005;21:177-201 PMID: 16212492
  20. BSKs mediate signal transduction from the receptor kinase BRI1 in Arabidopsis.
    Science. 2008 Jul 25;321(5888):557-60 PMID: 18653891
  21. Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.
    Dev Cell. 2008 Aug;15(2):220-35 PMID: 18694562
  22. BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana.
    Proc Natl Acad Sci U S A. 2001 May 8;98(10):5916-21 PMID: 11320207
  23. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex.
    Nature. 2009 Apr 30;458(7242):1191-5 PMID: 19252480
  24. BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.
    Cell. 2002 Jul 26;110(2):213-22 PMID: 12150929
  25. A brassinosteroid-hypersensitive mutant of BAK1 indicates that a convergence of photomorphogenic and hormonal signaling modulates phototropism.
    Plant Physiol. 2005 Sep;139(1):448-57 PMID: 16126860
  26. Brassinosteroid signaling: from receptor kinases to transcription factors.
    Curr Opin Plant Biol. 2005 Oct;8(5):526-31 PMID: 16054433
  27. Processing of X-ray diffraction data collected in oscillation mode.
    Methods Enzymol. 1997;276:307-26 PMID: 27754618
  28. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.
    Cell. 2002 Dec 13;111(6):825-36 PMID: 12526809
  29. Brassinosteroid signal transduction from receptor kinases to transcription factors.
    Annu Rev Plant Biol. 2010;61:681-704 PMID: 20192752
  30. PHENIX: building new software for automated crystallographic structure determination.
    Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54 PMID: 12393927
  31. Structural diversity of leucine-rich repeat proteins.
    J Mol Biol. 1998 Apr 3;277(3):519-27 PMID: 9533877
  32. Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis reveals amino acid residues critical for receptor formation and activation of BR signaling.
    Mol Cells. 2009 Feb 28;27(2):183-90 PMID: 19277500
  33. BRASSINOSTEROIDS: Essential Regulators of Plant Growth and Development.
    Annu Rev Plant Physiol Plant Mol Biol. 1998 Jun;49:427-451 PMID: 15012241
  34. Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor.
    Genes Dev. 2011 Feb 1;25(3):232-7 PMID: 21289069
Article Info
Journal
Nature
Abbr.
Nature
ISSN
1476-4687
DOI
10.1038/nature10178
Published
2011-06-12
Epub
2011-00-12
Pages
472-6
Language
English
Region
England
NLM ID
0410462
PMCID
PMC4019668
Subset
IM
Grants
NIGMS NIH HHS · R01 GM066258 · United States
NIGMS NIH HHS · R01GM066258 · United States
Databases
PDB
3RGX, 3RGZ
External Links
PubMed source DOI: 10.1038/nature10178 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2