A 5-Enolpyruvylshikimate 3-Phosphate Synthase Functions as a Transcriptional Repressor in Populus . Issue 7 (11th June 2018)
- Record Type:
- Journal Article
- Title:
- A 5-Enolpyruvylshikimate 3-Phosphate Synthase Functions as a Transcriptional Repressor in Populus . Issue 7 (11th June 2018)
- Main Title:
- A 5-Enolpyruvylshikimate 3-Phosphate Synthase Functions as a Transcriptional Repressor in Populus
- Authors:
- Xie, Meng
Muchero, Wellington
Bryan, Anthony C.
Yee, Kelsey
Guo, Hao-Bo
Zhang, Jin
Tschaplinski, Timothy J.
Singan, Vasanth R.
Lindquist, Erika
Payyavula, Raja S.
Barros-Rios, Jaime
Dixon, Richard
Engle, Nancy
Sykes, Robert W.
Davis, Mark
Jawdy, Sara S.
Gunter, Lee E.
Thompson, Olivia
DiFazio, Stephen P.
Evans, Luke M.
Winkeler, Kim
Collins, Cassandra
Schmutz, Jeremy
Guo, Hong
Kalluri, Udaya
Rodriguez, Miguel
Feng, Kai
Chen, Jin-Gui
Tuskan, Gerald A. - Abstract:
- Abstract : An isoform of the EPSP synthase enzyme possesses a DNA-binding helix-turn-helix motif and has dual roles in shikimate biosynthesis and transcriptional repressor activity. Abstract: Long-lived perennial plants, with distinctive habits of inter-annual growth, defense, and physiology, are of great economic and ecological importance. However, some biological mechanisms resulting from genome duplication and functional divergence of genes in these systems remain poorly studied. Here, we discovered an association between a poplar ( Populus trichocarpa) 5-enolpyruvylshikimate 3-phosphate synthase gene ( PtrEPSP ) and lignin biosynthesis. Functional characterization of PtrEPSP revealed that this isoform possesses a helix-turn-helix motif in the N terminus and can function as a transcriptional repressor that regulates expression of genes in the phenylpropanoid pathway in addition to performing its canonical biosynthesis function in the shikimate pathway. We demonstrated that this isoform can localize in the nucleus and specifically binds to the promoter and represses the expression of a SLEEPER -like transcriptional regulator, which itself specifically binds to the promoter and represses the expression of PtrMYB021 (known as MYB46 in Arabidopsis thaliana ), a master regulator of the phenylpropanoid pathway and lignin biosynthesis. Analyses of overexpression and RNAi lines targeting PtrEPSP confirmed the predicted changes in PtrMYB021 expression patterns. These resultsAbstract : An isoform of the EPSP synthase enzyme possesses a DNA-binding helix-turn-helix motif and has dual roles in shikimate biosynthesis and transcriptional repressor activity. Abstract: Long-lived perennial plants, with distinctive habits of inter-annual growth, defense, and physiology, are of great economic and ecological importance. However, some biological mechanisms resulting from genome duplication and functional divergence of genes in these systems remain poorly studied. Here, we discovered an association between a poplar ( Populus trichocarpa) 5-enolpyruvylshikimate 3-phosphate synthase gene ( PtrEPSP ) and lignin biosynthesis. Functional characterization of PtrEPSP revealed that this isoform possesses a helix-turn-helix motif in the N terminus and can function as a transcriptional repressor that regulates expression of genes in the phenylpropanoid pathway in addition to performing its canonical biosynthesis function in the shikimate pathway. We demonstrated that this isoform can localize in the nucleus and specifically binds to the promoter and represses the expression of a SLEEPER -like transcriptional regulator, which itself specifically binds to the promoter and represses the expression of PtrMYB021 (known as MYB46 in Arabidopsis thaliana ), a master regulator of the phenylpropanoid pathway and lignin biosynthesis. Analyses of overexpression and RNAi lines targeting PtrEPSP confirmed the predicted changes in PtrMYB021 expression patterns. These results demonstrate that PtrEPSP in its regulatory form and PtrhAT form a transcriptional hierarchy regulating phenylpropanoid pathway and lignin biosynthesis in Populus . … (more)
- Is Part Of:
- The Plant Cell. Volume 30:Issue 7(2018)
- Journal:
- The Plant Cell
- Issue:
- Volume 30:Issue 7(2018)
- Issue Display:
- Volume 30, Issue 7 (2018)
- Year:
- 2018
- Volume:
- 30
- Issue:
- 7
- Issue Sort Value:
- 2018-0030-0007-0000
- Page Start:
- 1645
- Page End:
- 1660
- Publication Date:
- 2018-06-11
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.18.00168 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19593.xml