ArticlePloS one2014
eEF1A is an S-RNase binding factor in self-incompatible Solanum chacoense.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- S-RNase-based self-incompatibility in angiosperms: Degradation, condensation, and evolution.Plant physiology · 2025Review
- Molecular mechanisms and genetic regulation of self-incompatibility in flowering plants: implications for crop improvement and evolutionary biology.Plant molecular biology · 2025Review
- Self-(In)compatibility Systems: Target Traits for Crop-Production, Plant Breeding, and Biotechnology.Frontiers in plant science · 2020Review
- Overcoming Self-Incompatibility in Diploid Potato Using CRISPR-Cas9.Frontiers in plant science · 2019Article
- Phosphatidic Acid Counteracts S-RNase Signaling in Pollen by Stabilizing the Actin Cytoskeleton.The Plant cell · 2018Article
- Live and Let Die: Phosphatidic Acid Modulates the Self-Incompatibility Response.The Plant cell · 2018Article
- Review
- SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida.Frontiers in genetics · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-incompatibility (SI) is a genetic mechanism that allows flowering plants to identify and block fertilization by self-pollen. In the Solanaceae, SI is controlled by a multiallelic S-locus encoding both S-RNases and F-box proteins as female and male determinants, respectively. S-RNase activity is essential for pollen rejection, and a minimum threshold value of S-RNases in the style is also required. Here we present biochemical evidence that eEF1A is a novel S-RNase-binding partner in vitro. We further show that the normal actin binding activity of eEF1A is enhanced by the presence of S-RNase. Lastly, we find that there is a co-localization of S-RNase and actin in the incompatible pollen tubes in structures reminiscent of the actin bundles formed by eEF1A. We propose that increased binding of eEF1A to actin in the presence of S-RNase could help explain the disruption of the actin cytoskeleton observed during SI reactions.
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