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. ISSN 1074-5521

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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
Volume:	Vol.18
Number:	No.4
Page Range:	pp. 542-552
Identification Number:	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)
URI:	http://wrap.warwick.ac.uk/id/eprint/40403

Data sourced from Thomson Reuters' Web of Knowledge

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