Expression of Brassica napus GLO1 is sufficient to breakdown artificial self-incompatibility in Arabidopsis thaliana

Plant Reprod. 2020 Dec;33(3-4):159-171. doi: 10.1007/s00497-020-00392-y. Epub 2020 Aug 29.

Abstract

Members of the Brassicaceae family have the ability to regulate pollination events occurring on the stigma surface. In Brassica species, self-pollination leads to an allele-specific interaction between the pollen small cysteine-rich peptide ligand (SCR/SP11) and the stigmatic S-receptor kinase (SRK) that activates the E3 ubiquitin ligase ARC1 (Armadillo repeat-containing 1), resulting in proteasomal degradation of various compatibility factors including glyoxalase I (GLO1) which is necessary for successful pollination. In Brassica napus, the suppression of GLO1 was sufficient to reduce compatibility, and overexpression of GLO1 in self-incompatible Brassica napus stigmas resulted in partial breakdown of the self-incompatibility response. Here, we verified if BnGLO1 could function as a compatibility factor in the artificial self-incompatibility system of Arabidopsis thaliana expressing AlSCRb, AlSRKb and AlARC1 proteins from A. lyrata. Overexpression of BnGLO1 is sufficient to breakdown self-incompatibility response in A. thaliana stigmas. Therefore, GLO1 has an indisputable role as a compatibility factor in the stigma in regulating pollen attachment and pollen tube growth. Lastly, this study demonstrates the usefulness of an artificial self-incompatibility system in A. thaliana for interspecific self-incompatibility studies.

Keywords: Arabidopsis; Brassica; Glyoxalase I; Pollen–pistil interactions; Pollination; Self-incompatibility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis* / genetics
  • Arabidopsis* / metabolism
  • Brassica napus* / genetics
  • Gene Expression Regulation, Plant*
  • Lactoylglutathione Lyase* / genetics
  • Plant Proteins* / genetics
  • Plants, Genetically Modified / metabolism
  • Self-Incompatibility in Flowering Plants* / genetics

Substances

  • Plant Proteins
  • Lactoylglutathione Lyase