scholarly journals Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana

2019 ◽  
Vol 70 (5) ◽  
pp. 1483-1495 ◽  
Author(s):  
Stephan Pollmann ◽  
Armin Springer ◽  
Sachin Rustgi ◽  
Diter von Wettstein ◽  
ChulHee Kang ◽  
...  
2009 ◽  
Vol 38 (1) ◽  
pp. 265-278 ◽  
Author(s):  
Katarzyna Dorota Raczynska ◽  
Craig G. Simpson ◽  
Adam Ciesiolka ◽  
Lukasz Szewc ◽  
Dominika Lewandowska ◽  
...  

1997 ◽  
Vol 11 (1) ◽  
pp. 73-82 ◽  
Author(s):  
H.E. Neuhaus ◽  
E. Thom ◽  
T. Mohlmann ◽  
M. Steup ◽  
K. Kampfenkel

PLoS Genetics ◽  
2018 ◽  
Vol 14 (2) ◽  
pp. e1007218 ◽  
Author(s):  
Na Li ◽  
Zupei Liu ◽  
Zhibiao Wang ◽  
Licong Ru ◽  
Nathalie Gonzalez ◽  
...  

2013 ◽  
Vol 91 ◽  
pp. 73-83 ◽  
Author(s):  
Christof Behrens ◽  
Christian Blume ◽  
Michael Senkler ◽  
Holger Eubel ◽  
Christoph Peterhänsel ◽  
...  

2021 ◽  
Author(s):  
Justin Michael Watkins ◽  
Alan M. Jones ◽  
Justin Walley ◽  
Natalie M Clark ◽  
Daisuke Urano ◽  
...  

flg22 is a 22 amino peptide released from bacterial flagellin a Microbe Associated Molecular 51 Pattern ( that is recognized by the plant cell as a signal indicating that bacteria are present. On its own, flg22 initiates a rapid increase in cytoplasmic calcium, extracellular reactive oxygen species, and activation of a Mitogen Activated Protein Kinase (cascade all of which are activated within 15 minutes after the cell perceives flg22. Here we show a massive change in protein abundance and phosphorylation state of the Arabidopsis root cell proteome within this 15 minute duration in wildtype and a mutant deficient in G protein coupled signaling Integration of phosphoproteome with protein protein interactome data followed by network topology analyses discovered that many of the flg22 induced phosphoproteome changes fall on proteins that comprise the G protein interactome and on the most highly populated hubs of the immunity network approximately 95% of the phosphorylation changes in the G protein interactome depend on a functional heterotrimeric G protein complex some occur on proteins that interact directly with components of G coupled signal transduction. One of these is ATBα, a substrate recognition sub-unit of the PP2A Ser/Thr phosphatase and an interactor to Arabidopsis thaliana REGULATOR OF G SIGNALING 1 protein (a 7 transmembrane spanning modulator of the nucleotide binding state of the core G protein complex. AtRGS1 is phosphorylated by BAK1, a component of the flg22 receptor, to initiate AtRGS1 endocytosis. A null mutation of ATB α confer s high 67 basal endocytosis of AtRGS1 suggesting sustained phosphorylated status. Loss of ATB α confers 68 trait s associated with loss of AtRGS1. Because the basal level of AtRGS1 is lower in the atbα null mutant in a proteasome dependent manner we propose that phosphorylation dependent endocytosis of AtRGS1 is part of a mechanism to degrade AtRGS1 which then sustains activation of the 71 G protein complex Thus, the role of ATB α is now established as a central component of phosphorylation dependent regulation of system dynamics in innate immunity


2006 ◽  
Vol 103 (39) ◽  
pp. 14631-14636 ◽  
Author(s):  
C. C. Wood ◽  
M. Robertson ◽  
G. Tanner ◽  
W. J. Peacock ◽  
E. S. Dennis ◽  
...  

2011 ◽  
Vol 53 (1) ◽  
pp. 125-134 ◽  
Author(s):  
Mizuki Yamaguchi ◽  
Katsuaki Takechi ◽  
Fumiyoshi Myouga ◽  
Shinya Imura ◽  
Hiroshi Sato ◽  
...  

2020 ◽  
Author(s):  
Ghazanfar Abbas Khan ◽  
Jules Deforges ◽  
Rodrigo S. Reis ◽  
Yi-Fang Hsieh ◽  
Jonatan Montpetit ◽  
...  

AbstractTranscription termination has important regulatory functions, impacting mRNA stability, localization and translation potential. Failure to appropriately terminate transcription can also lead to read-through transcription and the synthesis of antisense RNAs which can have profound impact on gene expression. The Transcription-Export (THO/TREX) protein complex plays an important role in coupling transcription with splicing and export of mRNA. However, little is known about the role of the THO/TREX complex in the control of transcription termination. In this work, we show that two proteins of the THO/TREX complex, namely TREX COMPONENT 1 (TEX1 or THO3) and HYPER RECOMBINATION1 (HPR1 or THO1) contribute to the correct transcription termination at several loci in Arabidopsis thaliana. We first demonstrate this by showing defective termination in tex1 and hpr1 mutants at the nopaline synthase (NOS) terminator present in a T-DNA inserted between exon 1 and 3 of the PHO1 locus in the pho1-7 mutant. Read-through transcription beyond the NOS terminator and splicing-out of the T-DNA resulted in the generation of a near full-length PHO1 mRNA (minus exon 2) in the tex1 pho1-7 and hpr1 pho1-7 double mutants, with enhanced production of a truncated PHO1 protein that retained phosphate export activity. Consequently, the strong reduction of shoot growth associated with the severe phosphate deficiency of the pho1-7 mutant was alleviated in the tex1 pho1-7 and hpr1 pho1-7 double mutants. Additionally, we show that RNA termination defects in tex1 and hpr1 mutants leads to 3’UTR extensions in several plant genes. These results demonstrate that THO/TREX complex contributes to the regulation of transcription termination.Author summaryProduction of messenger RNAs (mRNAs) involves numerous steps including initiation of transcription, elongation, splicing, termination, as well as export out of the nucleus. All these steps are highly coordinated and failure in any steps has a profound impact on the level and identity of mRNAs produced. The THO/TREX protein complex is associated with nascent RNAs and contributes to several mRNA biogenesis steps, including splicing and export. However, the contribution of the THO/TREX complex to mRNA termination was poorly defined. We have identified a role for two components of the THO/TREX complex, namely the proteins TEX1 and HPR1, in the control of transcription termination in the plant Arabidopsis thaliana. We show that the tex1 and hpr1 mutants have defects in terminating mRNA at the nopaline synthase (NOS) terminator found in T-DNA insertion mutants leading to the transcriptional read-through pass the NOS terminator. We also show that tex1 and hpr1 mutants have defects in mRNA termination at several endogenous genes, leading to the production of 3’UTR extensions. Together, these results highlight a role for the THO/TREX complex in mRNA termination.


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