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Electrostatic potentials of the S-locus F-box proteins contribute to the pollen S specificity in self-incompatibility in Petunia hybrida.
Plant J. 2017 01; 89(1):45-57.PJ

Abstract

Self-incompatibility (SI) is a self/non-self discrimination system found widely in angiosperms and, in many species, is controlled by a single polymorphic S-locus. In the Solanaceae, Rosaceae and Plantaginaceae, the S-locus encodes a single S-RNase and a cluster of S-locus F-box (SLF) proteins to control the pistil and pollen expression of SI, respectively. Previous studies have shown that their cytosolic interactions determine their recognition specificity, but the physical force between their interactions remains unclear. In this study, we show that the electrostatic potentials of SLF contribute to the pollen S specificity through a physical mechanism of 'like charges repel and unlike charges attract' between SLFs and S-RNases in Petunia hybrida. Strikingly, the alteration of a single C-terminal amino acid of SLF reversed its surface electrostatic potentials and subsequently the pollen S specificity. Collectively, our results reveal that the electrostatic potentials act as a major physical force between cytosolic SLFs and S-RNases, providing a mechanistic insight into the self/non-self discrimination between cytosolic proteins in angiosperms.

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Authors+Show Affiliations

Li J
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. University of Chinese Academy of Sciences, Beijing, 100190, China.
Zhang Y
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. University of Chinese Academy of Sciences, Beijing, 100190, China.
Song Y
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. University of Chinese Academy of Sciences, Beijing, 100190, China.
Zhang H
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. University of Chinese Academy of Sciences, Beijing, 100190, China.
Fan J
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. University of Chinese Academy of Sciences, Beijing, 100190, China.
Li Q
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China.
Zhang D
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China.
Xue Y
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research, Beijing, 100101, China. Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, 100101, China. Collaborative Innovation Center for Genetics and Development, Fudan University, Shanghai, 200433, China.

MeSH

F-Box ProteinsGene Expression Regulation, PlantHydrophobic and Hydrophilic InteractionsModels, MolecularMutationPetuniaPlant ProteinsPlants, Genetically ModifiedPollenPolyubiquitinProtein BindingProtein DomainsReverse Transcriptase Polymerase Chain ReactionRibonucleasesSelf-Incompatibility in Flowering PlantsStatic Electricity

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

27569591

Citation

Li, Junhui, et al. "Electrostatic Potentials of the S-locus F-box Proteins Contribute to the Pollen S Specificity in Self-incompatibility in Petunia Hybrida." The Plant Journal : for Cell and Molecular Biology, vol. 89, no. 1, 2017, pp. 45-57.
Li J, Zhang Y, Song Y, et al. Electrostatic potentials of the S-locus F-box proteins contribute to the pollen S specificity in self-incompatibility in Petunia hybrida. Plant J. 2017;89(1):45-57.
Li, J., Zhang, Y., Song, Y., Zhang, H., Fan, J., Li, Q., Zhang, D., & Xue, Y. (2017). Electrostatic potentials of the S-locus F-box proteins contribute to the pollen S specificity in self-incompatibility in Petunia hybrida. The Plant Journal : for Cell and Molecular Biology, 89(1), 45-57. https://doi.org/10.1111/tpj.13318
Li J, et al. Electrostatic Potentials of the S-locus F-box Proteins Contribute to the Pollen S Specificity in Self-incompatibility in Petunia Hybrida. Plant J. 2017;89(1):45-57. PubMed PMID: 27569591.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Electrostatic potentials of the S-locus F-box proteins contribute to the pollen S specificity in self-incompatibility in Petunia hybrida. AU - Li,Junhui, AU - Zhang,Yue, AU - Song,Yanzhai, AU - Zhang,Hui, AU - Fan,Jiangbo, AU - Li,Qun, AU - Zhang,Dongfen, AU - Xue,Yongbiao, Y1 - 2016/11/14/ PY - 2016/04/14/received PY - 2016/08/04/revised PY - 2016/08/22/accepted PY - 2016/8/30/pubmed PY - 2017/11/29/medline PY - 2016/8/30/entrez KW - Petunia hybrida KW - SLF KW - S-RNase KW - electrostatic potentials KW - pollen S specificity KW - self-incompatibility SP - 45 EP - 57 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 89 IS - 1 N2 - Self-incompatibility (SI) is a self/non-self discrimination system found widely in angiosperms and, in many species, is controlled by a single polymorphic S-locus. In the Solanaceae, Rosaceae and Plantaginaceae, the S-locus encodes a single S-RNase and a cluster of S-locus F-box (SLF) proteins to control the pistil and pollen expression of SI, respectively. Previous studies have shown that their cytosolic interactions determine their recognition specificity, but the physical force between their interactions remains unclear. In this study, we show that the electrostatic potentials of SLF contribute to the pollen S specificity through a physical mechanism of 'like charges repel and unlike charges attract' between SLFs and S-RNases in Petunia hybrida. Strikingly, the alteration of a single C-terminal amino acid of SLF reversed its surface electrostatic potentials and subsequently the pollen S specificity. Collectively, our results reveal that the electrostatic potentials act as a major physical force between cytosolic SLFs and S-RNases, providing a mechanistic insight into the self/non-self discrimination between cytosolic proteins in angiosperms. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/27569591/Electrostatic_potentials_of_the_S_locus_F_box_proteins_contribute_to_the_pollen_S_specificity_in_self_incompatibility_in_Petunia_hybrida_ DB - PRIME DP - Unbound Medicine ER -