Screen for soil fungi highly resistant to dichloroaniline uncovers mostly Fusarium species

Tong, L.; Dairou, Julien; Bui, Linh‐Chi; Bouillon, Julien; Rodrigues‐Lima, Fernando; Dupret, Jean‐Marie; Silar, Philippe

doi:10.1016/j.fgb.2015.05.011

Cited by 7 publications

(1 citation statement)

References 17 publications

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“…Although the literature has described NAT genes and their recombinant enzymatic products for several bacteria [5,7,9,[17][18][19][20][21][22][23][24][25][26][27][28][29], much less is known about NAT function in eukaryotic microorganisms, such as fungi. A few studies have investigated fungal NAT relative to the metabolism of xenobiotic arylamines, including certain by-products of agrochemicals [30][31][32]. However, the most comprehensive knowledge about the biological role of fungal NAT genes comes from studies of plant pathogens, implicating one particular Fusarium homologue in the detoxification of naturally occurring benzoxazinoids (BXs) [6,[33][34][35].…”

Section: Introductionmentioning

confidence: 99%

Fusarium verticillioidesNAT1 (FDB2) N‐malonyltransferase is structurally, functionally and phylogenetically distinct from its N‐acetyltransferase (NAT) homologues

et al. 2022

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Bob was a keen scientist who generously offered his expertise and patiently guided us through the complexities of protein work during this project, always ready to leave his desk for the bench. He is deeply missed.Fusarium endophytes damage cereal crops and contaminate produce with mycotoxins. Those fungi overcome the main chemical defence of host via detoxification by a malonyl-CoA-dependent enzyme homologous to xenobiotic metabolizing arylamine N-acetyltransferase (NAT). In Fusarium verticillioides (teleomorph Gibberella moniliformis, GIBMO), this Nmalonyltransferase activity is attributed to (GIBMO)NAT1, and the fungus has two additional isoenzymes, (GIBMO)NAT3 (N-acetyltransferase) and (GIBMO)NAT2 (unknown function). We present the crystallographic structure of (GIBMO)NAT1, also modelling other fungal NAT homologues. Monomeric (GIBMO)NAT1 is distinctive, with access to the catalytic core through two "tunnel-like" entries separated by a "bridge-like" helix. In the quaternary arrangement, (GIBMO)NAT1 monomers interact in pairs along an extensive interface whereby one entry of each monomer is covered by the N-terminus of the other monomer. Although monomeric (GIBMO)NAT1 apparently accommodates acetyl-CoA better than malonyl-CoA, dimerization changes the active site to allow malonyl-CoA to reach the catalytic triad (Cys110, His158 and Asp173) via the single uncovered entry, and anchor its terminal carboxyl-group via hydrogen bonds to Arg109, Asn157 and Thr261. Lacking a terminal carboxyl-group, acetyl-CoA cannot form such stabilizing interactions, while longer acyl-CoAs enter the active site but cannot reach catalytic Cys. Other NAT isoenzymes lack such structural features, with (GIBMO)NAT3 resembling bacterial NATs and (GIBMO)NAT2 adopting a structure intermediate between (GIBMO)NAT1 and (GIBMO)NAT3. Biochemical assays

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