Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1
Both animals and plants use steroids as signalling molecules during growth and development. Animal steroids are principally recognized by members of the nuclear receptor superfamily of transcription factors. In plants, BRI1, a leucine-rich repeat (LRR) receptor kinase localized to the plasma membran...
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| Veröffentlicht in: | Nature 2005-01, Vol.433 (7022), p.167-171 |
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| creator | Chory, Joanne Kinoshita, Toshinori Caño-Delgado, Ana Seto, Hideharu Hiranuma, Sayoko Fujioka, Shozo Yoshida, Shigeo |
| description | Both animals and plants use steroids as signalling molecules during growth and development. Animal steroids are principally recognized by members of the nuclear receptor superfamily of transcription factors. In plants, BRI1, a leucine-rich repeat (LRR) receptor kinase localized to the plasma membrane, is a critical component of a receptor complex for brassinosteroids. Here, we present the first evidence for direct binding of active brassinosteroids to BRI1 using a biotin-tagged photoaffinity castasterone (BPCS), a biosynthetic precursor of brassinolide (the most active of the brassinosteroids). Binding studies using BPCS, 3H-labelled brassinolide and recombinant BRI1 fragments show that the minimal binding domain for brassinosteroids consists of a 70-amino acid island domain (ID) located between LRR21 and LRR22 in the extracellular domain of BRI1, together with the carboxy-terminal flanking LRR (ID-LRR22). Our results demonstrate that brassinosteroids bind directly to the 94 amino acids comprising ID-LRR22 in the extracellular domain of BRI1, and define a new binding domain for steroid hormones. |
| doi_str_mv | 10.1038/nature03227 |
| format | Article |
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Animal steroids are principally recognized by members of the nuclear receptor superfamily of transcription factors. In plants, BRI1, a leucine-rich repeat (LRR) receptor kinase localized to the plasma membrane, is a critical component of a receptor complex for brassinosteroids. Here, we present the first evidence for direct binding of active brassinosteroids to BRI1 using a biotin-tagged photoaffinity castasterone (BPCS), a biosynthetic precursor of brassinolide (the most active of the brassinosteroids). Binding studies using BPCS, 3H-labelled brassinolide and recombinant BRI1 fragments show that the minimal binding domain for brassinosteroids consists of a 70-amino acid island domain (ID) located between LRR21 and LRR22 in the extracellular domain of BRI1, together with the carboxy-terminal flanking LRR (ID-LRR22). Our results demonstrate that brassinosteroids bind directly to the 94 amino acids comprising ID-LRR22 in the extracellular domain of BRI1, and define a new binding domain for steroid hormones.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature03227</identifier><identifier>PMID: 15650741</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Biological and medical sciences ; Biotin ; Biotin - metabolism ; Brassinosteroids ; Cholestanols - metabolism ; Cross-Linking Reagents ; Flowers & plants ; Fundamental and applied biological sciences. Psychology ; Growth regulators ; Hormones ; Humanities and Social Sciences ; letter ; Metabolism ; Molecular Sequence Data ; multidisciplinary ; Peptide Fragments - chemistry ; Peptide Fragments - genetics ; Peptide Fragments - metabolism ; Plant physiology and development ; Plants, Genetically Modified ; Protein Binding ; Protein Kinases - chemistry ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Protein Structure, Tertiary ; Science ; Science (multidisciplinary) ; Steroid hormones ; Steroids ; Steroids, Heterocyclic - metabolism</subject><ispartof>Nature, 2005-01, Vol.433 (7022), p.167-171</ispartof><rights>Macmillan Magazines Ltd. 2005</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2005 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. 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Animal steroids are principally recognized by members of the nuclear receptor superfamily of transcription factors. In plants, BRI1, a leucine-rich repeat (LRR) receptor kinase localized to the plasma membrane, is a critical component of a receptor complex for brassinosteroids. Here, we present the first evidence for direct binding of active brassinosteroids to BRI1 using a biotin-tagged photoaffinity castasterone (BPCS), a biosynthetic precursor of brassinolide (the most active of the brassinosteroids). Binding studies using BPCS, 3H-labelled brassinolide and recombinant BRI1 fragments show that the minimal binding domain for brassinosteroids consists of a 70-amino acid island domain (ID) located between LRR21 and LRR22 in the extracellular domain of BRI1, together with the carboxy-terminal flanking LRR (ID-LRR22). Our results demonstrate that brassinosteroids bind directly to the 94 amino acids comprising ID-LRR22 in the extracellular domain of BRI1, and define a new binding domain for steroid hormones.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biotin</subject><subject>Biotin - metabolism</subject><subject>Brassinosteroids</subject><subject>Cholestanols - metabolism</subject><subject>Cross-Linking Reagents</subject><subject>Flowers & plants</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Growth regulators</topic><topic>Hormones</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>Plant physiology and development</topic><topic>Plants, Genetically Modified</topic><topic>Protein Binding</topic><topic>Protein Kinases - chemistry</topic><topic>Protein Kinases - genetics</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Steroid hormones</topic><topic>Steroids</topic><topic>Steroids, Heterocyclic - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chory, Joanne</creatorcontrib><creatorcontrib>Kinoshita, Toshinori</creatorcontrib><creatorcontrib>Caño-Delgado, Ana</creatorcontrib><creatorcontrib>Seto, Hideharu</creatorcontrib><creatorcontrib>Hiranuma, Sayoko</creatorcontrib><creatorcontrib>Fujioka, Shozo</creatorcontrib><creatorcontrib>Yoshida, Shigeo</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Middle School</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Animal steroids are principally recognized by members of the nuclear receptor superfamily of transcription factors. In plants, BRI1, a leucine-rich repeat (LRR) receptor kinase localized to the plasma membrane, is a critical component of a receptor complex for brassinosteroids. Here, we present the first evidence for direct binding of active brassinosteroids to BRI1 using a biotin-tagged photoaffinity castasterone (BPCS), a biosynthetic precursor of brassinolide (the most active of the brassinosteroids). Binding studies using BPCS, 3H-labelled brassinolide and recombinant BRI1 fragments show that the minimal binding domain for brassinosteroids consists of a 70-amino acid island domain (ID) located between LRR21 and LRR22 in the extracellular domain of BRI1, together with the carboxy-terminal flanking LRR (ID-LRR22). Our results demonstrate that brassinosteroids bind directly to the 94 amino acids comprising ID-LRR22 in the extracellular domain of BRI1, and define a new binding domain for steroid hormones.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>15650741</pmid><doi>10.1038/nature03227</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Nature, 2005-01, Vol.433 (7022), p.167-171 |
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| language | eng |
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| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Amino acids Animals Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Biological and medical sciences Biotin Biotin - metabolism Brassinosteroids Cholestanols - metabolism Cross-Linking Reagents Flowers & plants Fundamental and applied biological sciences. Psychology Growth regulators Hormones Humanities and Social Sciences letter Metabolism Molecular Sequence Data multidisciplinary Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Plant physiology and development Plants, Genetically Modified Protein Binding Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Protein Structure, Tertiary Science Science (multidisciplinary) Steroid hormones Steroids Steroids, Heterocyclic - metabolism |
| title | Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1 |
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