Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1
| Autor: | Shozo Fujioka, Ana I. Caño-Delgado, Sayoko Hiranuma, Toshinori Kinoshita, Shigeo Yoshida, Hideharu Seto, Joanne Chory |
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| Rok vydání: | 2005 |
| Předmět: |
Receptor complex
Molecular Sequence Data Arabidopsis Biotin Plasma protein binding Biology chemistry.chemical_compound Steroids Heterocyclic Cell surface receptor Brassinosteroids Brassinosteroid Amino Acid Sequence Transcription factor Brassinolide Multidisciplinary Arabidopsis Proteins fungi Cell Biology Plants Genetically Modified Peptide Fragments Protein Structure Tertiary Cross-Linking Reagents chemistry Biochemistry Nuclear receptor Protein Kinases Cholestanols Protein Binding Binding domain |
| Zdroj: | Nature. 433:167-171 |
| ISSN: | 1476-4679 0028-0836 |
| Popis: | 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, (3)H-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. |
| Databáze: | OpenAIRE |
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