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 405681
Title The Aspartic Proteinase Family of Three Phytophthora Species
Author(s) Meijer, H.J.G.; Kay, J.; Have, A. ten; Govers, F.; Kan, J.A.L. van
Source In: Book of Abstracts Oomycete Molecular Genetics Network Meeting, Asilomar, Pacific Grove, California, USA, 13-15 March 2011. - - p. 26 - 26.
Event Oomycete Molecular Genetics Network Meeting 2011, Pacific Grove, 2011-03-13/2011-03-15
Department(s) Laboratory of Phytopathology
Publication type Abstract in scientific journal or proceedings
Publication year 2011
Abstract Pepsin-like aspartic proteinases (APs) are produced in a wide variety of species and contain conserved motifs and landmark residues. APs fulfil critical roles in infectious organisms and their host cells. Phytophthora species are oomycete plant pathogens with major social and economic impact. Several of which have been sequenced. The genomes ofPhytophthora infestans, P. sojae and P. ramorum contain 11-12 genes encoding APs, resolved into 5 cladcs by phylogenetic analysis. Several subfamilies contain an unconventional architecture, as they either lack a signal peptide or a propart region. One of the Phytophthora APs is an unprecedented fusion protein with a putative G-protein coupled receptor as the C-terminal partner. The others appear to be related to welldocumented enzymes from other species including a vacuolar enzyme that is encoded in every fungal genome sequenced to date. The oomycetes also have enzymes similar to plasmepsin V, a membrane-bound AP in the malaria parasite Plasmodium falciparum, that cleaves effector proteins during their translocation into the host red blood cell. The translocation of Phytophthora effectors to host cells is topic of intense research in which APs might be involved
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