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The role of glutathione S-transferase GliG in gliotoxin biosynthesis in aspergillus fumigatus

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Davis, Carol, Carberry, Stephen, Schrettl, Markus, Singh, Ishwar, Stephens, John C., Barry, Sarah M., Kavanagh, Kevin, Challis, Gregory L., Brougham, Dermot and Doyle, S. (Sean) (2011) The role of glutathione S-transferase GliG in gliotoxin biosynthesis in aspergillus fumigatus. Chemistry & Biology, Vol.18 (No.4). pp. 542-552. doi:10.1016/j.chembiol.2010.12.022

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Official URL: http://dx.doi.org/10.1016/j.chembiol.2010.12.022

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Abstract

Gliotoxin, a redox-active metabolite, is produced by the opportunistic fungal pathogen Aspergillus fumigatus, and its biosynthesis is directed by the gli gene cluster. Knowledge of the biosynthetic pathway to gliotoxin, which contains a disulfide bridge of unknown origin, is limited, although L-Phe and L-Ser are known biosynthetic precursors. Deletion of gliG from the gli cluster, herein functionally confirmed as a glutathione S-transferase, results in abrogation of gliotoxin biosynthesis and accumulation of 6-benzyl-6-hydroxy-1-methoxy-3-methylenepiperazine-2,5-dione. This putative shunt metabolite from the gliotoxin biosynthetic pathway contains an intriguing hydroxyl group at C-6, consistent with a gliotoxin biosynthetic pathway involving thiolation via addition of the glutathione thiol group to a reactive acyl imine intermediate. Complementation of gliG restored gliotoxin production and, unlike gliT, gliG was found not to be involved in fungal self-protection against gliotoxin.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QK Botany
Q Science > QP Physiology
Divisions: Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH): Aspergillus fumigatus, Mycotoxins -- Synthesis, Glutathione transferase
Journal or Publication Title: Chemistry & Biology
Publisher: Cell Press
ISSN: 1074-5521
Official Date: 22 April 2011
Dates:
DateEvent
22 April 2011Published
Volume: Vol.18
Number: No.4
Page Range: pp. 542-552
DOI: 10.1016/j.chembiol.2010.12.022
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Science Foundation Ireland (SFI), Programme for Research in Third-Level Institutions (PRTLI), European Commission (EC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC)
Grant number: RFP/GEN/F571 (SFI), BB/H006281/1 (BBSRC)

Data sourced from Thomson Reuters' Web of Knowledge

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