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The Arabidopsis Kinome

  • Background Protein kinases constitute a particularly large protein family in Arabidopsis with important functions in cellular signal transduction networks. At the same time Arabidopsis is a model plant with high frequencies of gene duplications. Here, we have conducted a systematic analysis of the Arabidopsis kinase complement, the kinome, with particular focus on gene duplication events. We matched Arabidopsis proteins to a Hidden-Markov Model of eukaryotic kinases and computed a phylogeny of 942 Arabidopsis protein kinase domains and mapped their origin by gene duplication. Results The phylogeny showed two major clades of receptor kinases and soluble kinases, each of which was divided into functional subclades. Based on this phylogeny, association of yet uncharacterized kinases to families was possible which extended functional annotation of unknowns. Classification of gene duplications within these protein kinases revealed that representatives of cytosolic subfamilies showed a tendency to maintain segmentally duplicatedBackground Protein kinases constitute a particularly large protein family in Arabidopsis with important functions in cellular signal transduction networks. At the same time Arabidopsis is a model plant with high frequencies of gene duplications. Here, we have conducted a systematic analysis of the Arabidopsis kinase complement, the kinome, with particular focus on gene duplication events. We matched Arabidopsis proteins to a Hidden-Markov Model of eukaryotic kinases and computed a phylogeny of 942 Arabidopsis protein kinase domains and mapped their origin by gene duplication. Results The phylogeny showed two major clades of receptor kinases and soluble kinases, each of which was divided into functional subclades. Based on this phylogeny, association of yet uncharacterized kinases to families was possible which extended functional annotation of unknowns. Classification of gene duplications within these protein kinases revealed that representatives of cytosolic subfamilies showed a tendency to maintain segmentally duplicated genes, while some subfamilies of the receptor kinases were enriched for tandem duplicates. Although functional diversification is observed throughout most subfamilies, some instances of functional conservation among genes transposed from the same ancestor were observed. In general, a significant enrichment of essential genes was found among genes encoding for protein kinases. Conclusions The inferred phylogeny allowed classification and annotation of yet uncharacterized kinases. The prediction and analysis of syntenic blocks and duplication events within gene families of interest can be used to link functional biology to insights from an evolutionary viewpoint. The approach undertaken here can be applied to any gene family in any organism with an annotated genome.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Monika Zulawski, Gunnar Schulze, Rostyslav Braginets, Stefanie HartmannORCiDGND, Waltraud X SchulzeORCiDGND
URN:urn:nbn:de:kobv:517-opus4-432907
DOI:https://doi.org/10.25932/publishup-43290
ISSN:1866-8372
Titel des übergeordneten Werks (Deutsch):Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe
Untertitel (Englisch):phylogeny and evolutionary insights into functional diversification
Schriftenreihe (Bandnummer):Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (861)
Publikationstyp:Postprint
Sprache:Englisch
Datum der Erstveröffentlichung:25.03.2020
Erscheinungsjahr:2014
Veröffentlichende Institution:Universität Potsdam
Datum der Freischaltung:25.03.2020
Freies Schlagwort / Tag:Duplication Event; Hide Markov Model; Kinase Family; Segmental Duplication; Tandem Duplication
Ausgabe:861
Seitenanzahl:17
Quelle:BMC Genomics 15 (2014) 548 DOI:10.1186/1471-2164-15-548
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät
DDC-Klassifikation:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Peer Review:Referiert
Publikationsweg:Open Access
Lizenz (Deutsch):License LogoCC-BY - Namensnennung 4.0 International
Externe Anmerkung:Bibliographieeintrag der Originalveröffentlichung/Quelle
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