Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/123901
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Type: Journal article
Title: Variation among S-locus haplotypes and among stylar RNases in almond
Author: Goonetilleke, S.N.
Croxford, A.E.
March, T.J.
Wirthensohn, M.G.
Hrmova, M.
Mather, D.E.
Citation: Scientific Reports, 2020; 10(1):583-1-583-15
Publisher: Springer Nature
Issue Date: 2020
ISSN: 2045-2322
2045-2322
Statement of
Responsibility: 
Shashi N. Goonetilleke, Adam E . Croxford, Timothy J. March, Michelle G. Wirthensohn, Maria Hrmova, Diane E. Mather
Abstract: In many plant species, self-incompatibility systems limit self-pollination and mating among relatives. This helps maintain genetic diversity in natural populations but imposes constraints in agriculture and plant breeding. In almond [Prunus dulcis (Mill.) D.A. Webb], the specificity of self-incompatibility is mainly determined by stylar ribonuclease (S-RNase) and S-haplotype-specific F-box (SFB) proteins, both encoded within a complex locus, S. Prior to this research, a nearly complete sequence was available for one S-locus haplotype. Here, we report complete sequences for four haplotypes and partial sequences for 11 haplotypes. Haplotypes vary in sequences of genes (particularly S-RNase and SFB), distances between genes and numbers and positions of long terminal repeat transposons. Haplotype variation outside of the S-RNase and SFB genes may help maintain functionally important associations between S-RNase and SFB alleles. Fluorescence-based assays were developed to distinguish among some S-RNase alleles. With three-dimensional modelling of five S-RNase proteins, conserved active sites were identified and variation was observed in electrostatic potential and in the numbers, characteristics and positions of secondary structural elements, loop anchoring points and glycosylation sites. A hypervariable region on the protein surface and differences in the number, location and types of glycosylation sites may contribute to determining S-RNase specificity.
Keywords: Ribonucleases; F-Box Proteins; Plant Proteins; Sequence Analysis, DNA; Catalytic Domain; Terminal Repeat Sequences; Protein Structure, Secondary; Glycosylation; Haplotypes; Models, Molecular; Genetic Loci; Prunus dulcis
Rights: © The Author(s) 2020. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
RMID: 1000013023
DOI: 10.1038/s41598-020-57498-6
Grant ID: http://purl.org/au-research/grants/arc/DP120100900
Appears in Collections:Agriculture, Food and Wine publications

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