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Exploring the Role of Trehalose‐6‐phosphate Synthase in Oxidation and Desiccation Stress Tolerance of Fusarium verticillioides
Author(s) -
Oberlie Nicole R.,
McMillan Sarah D.,
Pierson Paige N.,
Bonich Nicholas S.,
Brown Daren W.,
McQuade Kristi L.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.779.4
Subject(s) - trehalose , mutant , desiccation , biochemistry , enzyme , pathogenic fungus , atp synthase , biology , fusarium , conidiation , chemistry , microbiology and biotechnology , gene , botany
Fusarium verticillioides is a pathogenic filamentous fungus that primarily affects maize. We are exploring stress response mechanisms in F. verticillioides , particularly the role of the disaccharide trehalose. Trehalose‐6‐phosphate synthase, coded for by the TPS1 gene, catalyzes the first of two steps in trehalose synthesis. Past work in our lab indicated that an F. verticillioides Δtps1 mutant produces no trehalose and has reduced pathogenicity against maize. We report here that the Δtps1 mutant is sensitive to both oxidative and desiccation stress, suggesting a role for trehalose in stress tolerance. To determine if the stress sensitivity observed in this strain is due to the absence of trehalose or to the lack of a secondary function(s) of the enzyme, we are exploring stress response and sensitivity of a deletion mutant complemented with a mutant of TPS1 encoding a form of the enzyme expected to be catalytically inactive.