Ancient diversity of splicing motifs and protein surfaces in the wild emmer wheat (Triticum dicoccoides) LR10 coiled coil (CC) and leucine-rich repeat (LRR) domains

Hanan Sela, Laurentiu Spiridon, Andrei-Jose Petrescu, Martin Akerman, Yael Mandel-Gutfreund, Eviatar Nevo, Caroline Loutre, Beat Keller, Alan Schulman, Tzion Fahima

Research output: Contribution to journalArticleScientificpeer-review

Abstract

In this study, we explore the diversity and its distribution along the wheat leaf rust resistance protein LR10 three-dimensional structure. Lr10 is a leaf rust resistance gene encoding a coiled coil–nucleotide-binding site–leucine-rich repeat (CC–NBS–LRR) class of protein. Lr10 was cloned and sequenced from 58 accessions representing diverse habitats of wild emmer wheat in Israel. Nucleotide diversity was very high relative to other wild emmer wheat genes (π= 0.029). The CC domain was found to be the most diverse domain and subject to positive selection. Superimposition of the diversity on the CC three-dimensional structure showed that some of the variable and positively selected residues were solvent exposed and may interact with other proteins. The LRR domain was relatively conserved, but showed a hotspot of amino acid variation between two haplotypes in the ninth repeat. This repeat was longer than the other LRRs, and three-dimensional modelling suggested that an extensive α helix structure was formed in this region. The two haplotypes also differed in splicing regulation motifs. In genotypes with one haplotype, an intron was alternatively spliced in this region, whereas, in genotypes with the other haplotype, this intron did not splice at all. The two haplotypes are proposed to be ancient and maintained by balancing selection.
Original languageEnglish
JournalMolecular Plant Pathology
Volume13
Issue number3
Pages (from-to)276-287
Number of pages12
ISSN1464-6722
DOIs
Publication statusPublished - 2012
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 1183 Plant biology, microbiology, virology

Cite this

Sela, Hanan ; Spiridon, Laurentiu ; Petrescu, Andrei-Jose ; Akerman, Martin ; Mandel-Gutfreund, Yael ; Nevo, Eviatar ; Loutre, Caroline ; Keller, Beat ; Schulman, Alan ; Fahima, Tzion. / Ancient diversity of splicing motifs and protein surfaces in the wild emmer wheat (Triticum dicoccoides) LR10 coiled coil (CC) and leucine-rich repeat (LRR) domains. In: Molecular Plant Pathology. 2012 ; Vol. 13, No. 3. pp. 276-287.
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abstract = "In this study, we explore the diversity and its distribution along the wheat leaf rust resistance protein LR10 three-dimensional structure. Lr10 is a leaf rust resistance gene encoding a coiled coil–nucleotide-binding site–leucine-rich repeat (CC–NBS–LRR) class of protein. Lr10 was cloned and sequenced from 58 accessions representing diverse habitats of wild emmer wheat in Israel. Nucleotide diversity was very high relative to other wild emmer wheat genes (π= 0.029). The CC domain was found to be the most diverse domain and subject to positive selection. Superimposition of the diversity on the CC three-dimensional structure showed that some of the variable and positively selected residues were solvent exposed and may interact with other proteins. The LRR domain was relatively conserved, but showed a hotspot of amino acid variation between two haplotypes in the ninth repeat. This repeat was longer than the other LRRs, and three-dimensional modelling suggested that an extensive α helix structure was formed in this region. The two haplotypes also differed in splicing regulation motifs. In genotypes with one haplotype, an intron was alternatively spliced in this region, whereas, in genotypes with the other haplotype, this intron did not splice at all. The two haplotypes are proposed to be ancient and maintained by balancing selection.",
keywords = "1183 Plant biology, microbiology, virology",
author = "Hanan Sela and Laurentiu Spiridon and Andrei-Jose Petrescu and Martin Akerman and Yael Mandel-Gutfreund and Eviatar Nevo and Caroline Loutre and Beat Keller and Alan Schulman and Tzion Fahima",
year = "2012",
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Ancient diversity of splicing motifs and protein surfaces in the wild emmer wheat (Triticum dicoccoides) LR10 coiled coil (CC) and leucine-rich repeat (LRR) domains. / Sela, Hanan; Spiridon, Laurentiu; Petrescu, Andrei-Jose; Akerman, Martin; Mandel-Gutfreund, Yael; Nevo, Eviatar; Loutre, Caroline; Keller, Beat; Schulman, Alan; Fahima, Tzion.

In: Molecular Plant Pathology, Vol. 13, No. 3, 2012, p. 276-287.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Ancient diversity of splicing motifs and protein surfaces in the wild emmer wheat (Triticum dicoccoides) LR10 coiled coil (CC) and leucine-rich repeat (LRR) domains

AU - Sela, Hanan

AU - Spiridon, Laurentiu

AU - Petrescu, Andrei-Jose

AU - Akerman, Martin

AU - Mandel-Gutfreund, Yael

AU - Nevo, Eviatar

AU - Loutre, Caroline

AU - Keller, Beat

AU - Schulman, Alan

AU - Fahima, Tzion

PY - 2012

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N2 - In this study, we explore the diversity and its distribution along the wheat leaf rust resistance protein LR10 three-dimensional structure. Lr10 is a leaf rust resistance gene encoding a coiled coil–nucleotide-binding site–leucine-rich repeat (CC–NBS–LRR) class of protein. Lr10 was cloned and sequenced from 58 accessions representing diverse habitats of wild emmer wheat in Israel. Nucleotide diversity was very high relative to other wild emmer wheat genes (π= 0.029). The CC domain was found to be the most diverse domain and subject to positive selection. Superimposition of the diversity on the CC three-dimensional structure showed that some of the variable and positively selected residues were solvent exposed and may interact with other proteins. The LRR domain was relatively conserved, but showed a hotspot of amino acid variation between two haplotypes in the ninth repeat. This repeat was longer than the other LRRs, and three-dimensional modelling suggested that an extensive α helix structure was formed in this region. The two haplotypes also differed in splicing regulation motifs. In genotypes with one haplotype, an intron was alternatively spliced in this region, whereas, in genotypes with the other haplotype, this intron did not splice at all. The two haplotypes are proposed to be ancient and maintained by balancing selection.

AB - In this study, we explore the diversity and its distribution along the wheat leaf rust resistance protein LR10 three-dimensional structure. Lr10 is a leaf rust resistance gene encoding a coiled coil–nucleotide-binding site–leucine-rich repeat (CC–NBS–LRR) class of protein. Lr10 was cloned and sequenced from 58 accessions representing diverse habitats of wild emmer wheat in Israel. Nucleotide diversity was very high relative to other wild emmer wheat genes (π= 0.029). The CC domain was found to be the most diverse domain and subject to positive selection. Superimposition of the diversity on the CC three-dimensional structure showed that some of the variable and positively selected residues were solvent exposed and may interact with other proteins. The LRR domain was relatively conserved, but showed a hotspot of amino acid variation between two haplotypes in the ninth repeat. This repeat was longer than the other LRRs, and three-dimensional modelling suggested that an extensive α helix structure was formed in this region. The two haplotypes also differed in splicing regulation motifs. In genotypes with one haplotype, an intron was alternatively spliced in this region, whereas, in genotypes with the other haplotype, this intron did not splice at all. The two haplotypes are proposed to be ancient and maintained by balancing selection.

KW - 1183 Plant biology, microbiology, virology

U2 - 10.1111/j.1364-3703.2011.00744.x

DO - 10.1111/j.1364-3703.2011.00744.x

M3 - Article

VL - 13

SP - 276

EP - 287

JO - Molecular Plant Pathology

JF - Molecular Plant Pathology

SN - 1464-6722

IS - 3

ER -