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Structural basis for specific self-incompatibility response in Brassica.

Rui Ma1, Zhifu Han1, Zehan Hu1

  • 1Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

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|November 9, 2016
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Summary

Self-incompatibility in Brassica relies on S-locus receptor kinase (SRK) recognizing S-locus cysteine-rich protein (SCR). This study reveals the structural basis of SCR-SRK binding, explaining how it triggers receptor dimerization and SI specificity.

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Area of Science:

  • Plant reproductive biology
  • Molecular genetics
  • Structural biology

Background:

  • Self-incompatibility (SI) prevents self-fertilization in many flowering plants, including Brassica.
  • SI specificity is determined by the interaction between S-locus receptor kinase (SRK) and S-locus cysteine-rich protein (SCR).

Purpose of the Study:

  • To determine the crystal structure of the extracellular domain of SRK9 (eSRK9) in complex with SCR9.
  • To elucidate the structural mechanisms underlying the specific recognition between SCR and SRK.

Main Methods:

  • X-ray crystallography to obtain the 3D structure of the eSRK9-SCR9 complex.
  • Biochemical assays involving site-directed mutagenesis to assess the impact of specific residues on binding.

Main Results:

  • The crystal structure revealed a 2:2 eSRK:SCR heterotetramer with an "A" shape.
  • SCR binding induces eSRK9 homodimerization, mediated by interactions with hyper-variable regions of eSRK9.
  • Mutations in key interaction residues disrupted eSRK9-SCR9 binding in vitro.

Conclusions:

  • The study provides a structural basis for SCR-SRK recognition and SI specificity in Brassica.
  • The findings offer a structural template for understanding the co-evolution of SRK and SCR proteins.