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Glycogen metabolic genes are involved in trehalose-6-phosphate synthase-mediated regulation of pathogenicity by the rice blast fungus Magnaporthe oryzae.
Authors
AE Stellwagen
AJ Foster
+60 more
AM Carroll
B Valent
C Veneault-Fourrey
D Mayer
DB Rylatt
DG Saunders
DJ Ballance
E Thines
EH Fischer
G Giaever
GK Bhambra
HH Sillje
I Farkas
J Fernandez
JA Sweigard
JC de Jong
JD Thompson
JL Parrou
JL Parrou
JR Xu
K Adachi
K Lerch
KP Dixon
KR Oldenburg
Lucy J. Holcombe
MA Frohman
MA Teste
Michael J. Kershaw
MJ Kershaw
Muhammad Badaruddin
Nicholas J. Talbot
NJ Talbot
NL Catlett
NL Craig
P Kankanala
P Skamnioti
Peter N. Dodds
PK Hwang
PK Hwang
RA Dean
RA Wilson
RA Wilson
RA Wilson
RA Wilson
Richard A. Wilson
RJ Howard
RWS Weber
SF Altschul
SH Lillie
T Chida
TA Hardy
TK Mitchell
TM Bourett
WA Wilson
X Zhao
YZ Deng
YZ Deng
Z Gunja-Smith
Zheng-Yi Wang
ZY Wang
Publication date
3 October 2013
Publisher
'Public Library of Science (PLoS)'
Doi
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on
PubMed
Abstract
© 2013 Badaruddin et al.Editor - Peter N. Dodds, Commonwealth Scientific and Industrial Research Organisation (CSIRO), AustraliaThis work was funded by the Biotechnology and Biological Sciences Research Council and a European Research Council Advanced Investigator Award to NJT. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.The filamentous fungus Magnaporthe oryzae is the causal agent of rice blast disease. Here we show that glycogen metabolic genes play an important role in plant infection by M. oryzae. Targeted deletion of AGL1 and GPH1, which encode amyloglucosidase and glycogen phosphorylase, respectively, prevented mobilisation of glycogen stores during appressorium development and caused a significant reduction in the ability of M. oryzae to cause rice blast disease. By contrast, targeted mutation of GSN1, which encodes glycogen synthase, significantly reduced the synthesis of intracellular glycogen, but had no effect on fungal pathogenicity. We found that loss of AGL1 and GPH1 led to a reduction in expression of TPS1 and TPS3, which encode components of the trehalose-6-phosphate synthase complex, that acts as a genetic switch in M. oryzae. Tps1 responds to glucose-6-phosphate levels and the balance of NADP/NADPH to regulate virulence-associated gene expression, in association with Nmr transcriptional inhibitors. We show that deletion of the NMR3 transcriptional inhibitor gene partially restores virulence to a Δagl1Δgph1 mutant, suggesting that glycogen metabolic genes are necessary for operation of the NADPH-dependent genetic switch in M. oryzae.Biotechnology and Biological Sciences Research Council (BBSRC)European Research Council (ERC
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