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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 ISSN 1074-5521.
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Official URL: http://dx.doi.org/10.1016/j.chembiol.2010.12.022
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 |
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| Divisions: | Faculty of Science, Engineering and Medicine > 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: |
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| 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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