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 537998
Title The G-protein γ subunit of Phytophthora infestans is involved in sporangial development
Author(s) Hoogen, Johan van den; Verbeek-de Kruif, Natalie; Govers, Francine
Source Fungal Genetics and Biology 116 (2018). - ISSN 1087-1845 - p. 73 - 82.
DOI https://doi.org/10.1016/j.fgb.2018.04.012
Department(s) Laboratory of Phytopathology
EPS
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) G-protein subunit - GPCR - Oomycetes - Phytophthora - Signaling
Abstract

The oomycete Phytophthora infestans is a notorious plant pathogen with potato and tomato as its primary hosts. Previous research showed that the heterotrimeric G-protein subunits Gα and Gβ have a role in zoospore motility and virulence, and sporangial development, respectively. Here, we present analyses of the gene encoding a Gγ subunit in P. infestans, Pigpg1. The overall similarity of PiGPG1 with non-oomycete Gγ subunits is low, with only the most conserved amino acids maintained, but similarity with its homologs in other oomycetes is high. Pigpg1 is expressed in all life stages and shows a similar expression profile as the gene encoding the Gβ subunit, Pigpb1. To elucidate its function, transformants were generated in which Pigpg1 is silenced or overexpressed and their phenotypes were analyzed. Pigpg1-silenced lines produce less sporangia, which are malformed. Altogether, the results show that PiGPG1 is crucial for proper sporangia development and zoosporogenesis. PiGPG1 is a functional Gγ, and likely forms a dimer with PiGPB1 that mediates signaling.

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