Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 564003
Title Leucine-rich repeat receptor-like kinase II phylogenetics reveals five main clades throughout the plant kingdom
Author(s) Hosseini, Samin; Schmidt, Ed D.L.; Bakker, Freek T.
Source The Plant Journal 103 (2020)2. - ISSN 0960-7412 - p. 547 - 560.
Department(s) Biosystematics
Publication type Refereed Article in a scientific journal
Publication year 2020
Keyword(s) kinase - leucine-rich repeat receptor - LRR-RLKII - phylogeny - SERK

Receptor-like kinases (RLKs) represent the largest group of cell surface receptors in plants. The monophyletic leucine-rich repeat (LRR)-RLK subfamily II is considered to contain the somatic embryogenesis receptor kinases (SERKs) and NSP-interacting kinases known to be involved in developmental processes and cellular immunity in plants. There are only a few published studies on the phylogenetics of LRR-RLKII; unfortunately these suffer from poor taxon/gene sampling. Hence, it is not clear how many and what main clades this family contains, let alone what structure–function relationships exist. We used 1342 protein sequences annotated as ‘SERK’ and ‘SERK-like’ plus related sequences in order to estimate phylogeny within the LRR-RLKII clade, using the nematode protein kinase Pelle as an outgroup. We reconstruct five main clades (LRR-RLKII 1–5), in each of which the main pattern of land plant relationships re-occurs, confirming previous hypotheses that duplication events happened in this gene subfamily prior to divergence among land plant lineages. We show that domain structures and intron–exon boundaries within the five clades are well conserved in evolution. Furthermore, phylogenetic patterns based on the separate LRR and kinase parts of LRR-RLKs are incongruent: whereas the LRR part supports a LRR-RLKII 2/3 sister group relationship, the kinase part supports clades 1/2. We infer that the kinase part includes few ‘radical’ amino acid changes compared with the LRR part. Finally, our results confirm that amino acids involved in each LRR-RLKII–receptor complex interaction are located at N-capping residues, and that the short amino acid motifs of this interaction domain are highly conserved throughout evolution within the five LRR-RLKII clades.

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