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A subunit of the oligosaccharyltransferase complex is required for interspecific gametophyte recognition in Arabidopsis

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  • Lena M. Müller

    (University of Zürich
    Present address: Boyce-Thompson Institute for Plant Research, 533 Tower Road, Ithaca, New York 14853, USA)

  • Heike Lindner

    (University of Zürich
    Present address: Carnegie Institution for Science, Department of Plant Biology, 260 Panama Street, Stanford, California 94305, USA)

  • Nuno D. Pires

    (University of Zürich)

  • Valeria Gagliardini

    (University of Zürich)

  • Ueli Grossniklaus

    (University of Zürich)

Abstract

Species-specific gamete recognition is a key premise to ensure reproductive success and the maintenance of species boundaries. During plant pollen tube (PT) reception, gametophyte interactions likely allow the species-specific recognition of signals from the PT (male gametophyte) by the embryo sac (female gametophyte), resulting in PT rupture, sperm release, and double fertilization. This process is impaired in interspecific crosses between Arabidopsis thaliana and related species, leading to PT overgrowth and a failure to deliver the sperm cells. Here we show that ARTUMES (ARU) specifically regulates the recognition of interspecific PTs in A. thaliana. ARU, identified in a genome-wide association study (GWAS), exclusively influences interspecific—but not intraspecific—gametophyte interactions. ARU encodes the OST3/6 subunit of the oligosaccharyltransferase complex conferring protein N-glycosylation. Our results suggest that glycosylation patterns of cell surface proteins may represent an important mechanism of gametophyte recognition and thus speciation.

Suggested Citation

  • Lena M. Müller & Heike Lindner & Nuno D. Pires & Valeria Gagliardini & Ueli Grossniklaus, 2016. "A subunit of the oligosaccharyltransferase complex is required for interspecific gametophyte recognition in Arabidopsis," Nature Communications, Nature, vol. 7(1), pages 1-10, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10826
    DOI: 10.1038/ncomms10826
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