Comparative proteomic analyses reveal that the regulators of G‐protein signaling proteins regulate amino acid metabolism of the rice blast fungus Magnaporthe oryzae. Issue 21 (November 2014)
- Record Type:
- Journal Article
- Title:
- Comparative proteomic analyses reveal that the regulators of G‐protein signaling proteins regulate amino acid metabolism of the rice blast fungus Magnaporthe oryzae. Issue 21 (November 2014)
- Main Title:
- Comparative proteomic analyses reveal that the regulators of G‐protein signaling proteins regulate amino acid metabolism of the rice blast fungus Magnaporthe oryzae
- Authors:
- Zhang, Haifeng
Ma, Hongyu
Xie, Xin
Ji, Jun
Dong, Yanhan
Du, Yan
Tang, Wei
Zheng, Xiaobo
Wang, Ping
Zhang, Zhengguang - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The rice blast fungus <italic>Magnaporthe oryzae</italic> encodes eight regulators of G‐protein (GTP‐binding protein) signaling (RGS) proteins MoRgs1–MoRgs8 that orchestrate the growth, asexual/sexual production, appressorium differentiation, and pathogenicity. To address the mechanisms by which MoRgs proteins function, we conducted a 2DE proteome study and identified 82 differentially expressed proteins by comparing five ∆<italic>Morgs</italic> mutants with wild‐type Guy11 strain. We found that the abundances of eight amino acid (AA) biosynthesis or degradation associated proteins were markedly altered in five ∆<italic>Morgs</italic> mutants, indicating one of the main collective roles for the MoRgs proteins is to influence AA metabolism. We showed that MoRgs proteins have distinct roles in AA metabolism and nutrient responses from growth assays. In addition, we characterized MoLys20 (Lys is lysine), a homocitrate synthase, whose abundance was significantly decreased in the ∆<italic>Morgs</italic> mutants. The ∆<italic>Molys20</italic> mutant is auxotrophic for lys and exogenous lys could partially rescue its auxotrophic defects. Deletion of <italic>MoLYS20</italic> resulted in defects in conidiation and infection, as well as pathogenicity on rice. Overall, our results indicate that one of the critical roles for MoRgs proteins is to regulate AA metabolism, and that MoLys20 may be<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The rice blast fungus <italic>Magnaporthe oryzae</italic> encodes eight regulators of G‐protein (GTP‐binding protein) signaling (RGS) proteins MoRgs1–MoRgs8 that orchestrate the growth, asexual/sexual production, appressorium differentiation, and pathogenicity. To address the mechanisms by which MoRgs proteins function, we conducted a 2DE proteome study and identified 82 differentially expressed proteins by comparing five ∆<italic>Morgs</italic> mutants with wild‐type Guy11 strain. We found that the abundances of eight amino acid (AA) biosynthesis or degradation associated proteins were markedly altered in five ∆<italic>Morgs</italic> mutants, indicating one of the main collective roles for the MoRgs proteins is to influence AA metabolism. We showed that MoRgs proteins have distinct roles in AA metabolism and nutrient responses from growth assays. In addition, we characterized MoLys20 (Lys is lysine), a homocitrate synthase, whose abundance was significantly decreased in the ∆<italic>Morgs</italic> mutants. The ∆<italic>Molys20</italic> mutant is auxotrophic for lys and exogenous lys could partially rescue its auxotrophic defects. Deletion of <italic>MoLYS20</italic> resulted in defects in conidiation and infection, as well as pathogenicity on rice. Overall, our results indicate that one of the critical roles for MoRgs proteins is to regulate AA metabolism, and that MoLys20 may be directly or indirectly regulated by MoRgs and participated in lys biosynthesis, thereby affecting fungal development and pathogenicity.</p> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 14:Issue 21/22(2014)
- Journal:
- Proteomics
- Issue:
- Volume 14:Issue 21/22(2014)
- Issue Display:
- Volume 14, Issue 21/22 (2014)
- Year:
- 2014
- Volume:
- 14
- Issue:
- 21/22
- Issue Sort Value:
- 2014-0014-NaN-0000
- Page Start:
- 2508
- Page End:
- 2522
- Publication Date:
- 2014-11
- Subjects:
- Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201400173 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
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- 3774.xml