Evolution of GHF5 endoglucanase gene structure in plant-parasitic nematodes: no evidence for an early domain shuffling event

Tina Kyndt, Annelies Haegeman, Godelieve Gheysen

    Onderzoeksoutput: Bijdrage aan tijdschriftA1: Web of Science-artikel

    Uittreksel

    Endo-1,4-beta-glucanases or cellulases from the glycosyl hydrolase family 5 (GHF5) have been found in numerous bacteria and fungi, and recently also in higher eukaryotes, particularly in plant-parasitic nematodes (PPN). The origin of these genes has been attributed to horizontal gene transfer from bacteria, although there still is a lot of uncertainty about the origin and structure of the ancestral GHF5 PPN endoglucanase. It is not clear whether this ancestral endoglucanase consisted of the whole gene cassette, containing a catalytic domain and a carbohydrate-binding module (CBM, type 2 in PPN and bacteria) or only of the catalytic domain while the CBM2 was retrieved by domain shuffling later in evolution. Previous studies on the evolution of these genes have focused primarily on data of sedentary nematodes, while in this study, extra data from migratory nematodes were included.
    TaalEngels
    TijdschriftBMC Evolutionary Biology
    Volume8
    Pagina's (van-tot)305
    ISSN1471-2148
    DOI's
    StatusGepubliceerd - 2008

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