Evidence map›Paper›PMID 21952112›Full record

ArticleMolecular plant pathology2012

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

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Article in Molecular plant pathology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

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0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023
    Article
  4. Article
  5. Article
  6. A new comprehensive annotation of leucine-rich repeat-containing receptors in rice.The Plant journal : for cell and molecular biology · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Distribution and haplotype diversity of WKS resistance genes in wild emmer wheat natural populations.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Alternative splicing in plant immunity.International journal of molecular sciences · 2014
    Review
  20. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

10 authors.

Hanan SelaDepartment of Evolutionary and Environmental Biology, Institute of Evolution, University of Haifa, Mt. Carmel, Haifa 31905, Israel.
Laurentiu N Spiridon
Andrei-Jose Petrescu
Martin Akerman
Yael Mandel-Gutfreund
Eviatar Nevo
Caroline Loutre
Beat Keller
Alan H Schulman
Tzion Fahima

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Amino Acid SequenceBasidiomycotaMolecular Sequence DataPlant DiseasesPlant ImmunityPlant ProteinsProtein Structure, TertiarySequence Homology, Amino AcidTriticumPlant Proteins

Identifiers

PMID21952112
PMCPMC6638671

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.