The arabidopsis cyclic nucleotide interactome. Issue 1 (December 2016)
- Record Type:
- Journal Article
- Title:
- The arabidopsis cyclic nucleotide interactome. Issue 1 (December 2016)
- Main Title:
- The arabidopsis cyclic nucleotide interactome
- Authors:
- Donaldson, Lara
Meier, Stuart
Gehring, Christoph - Abstract:
- Abstract Background Cyclic nucleotides have been shown to play important signaling roles in many physiological processes in plants including photosynthesis and defence. Despite this, little is known about cyclic nucleotide-dependent signaling mechanisms in plants since the downstream target proteins remain unknown. This is largely due to the fact that bioinformatics searches fail to identify plant homologs of protein kinases and phosphodiesterases that are the main targets of cyclic nucleotides in animals. Methods An affinity purification technique was used to identify cyclic nucleotide binding proteins inArabidopsis thaliana . The identified proteins were subjected to a computational analysis that included a sequence, transcriptional co-expression and functional annotation analysis in order to assess their potential role in plant cyclic nucleotide signaling. Results A total of twelve cyclic nucleotide binding proteins were identified experimentally including key enzymes in the Calvin cycle and photorespiration pathway. Importantly, eight of the twelve proteins were shown to contain putative cyclic nucleotide binding domains. Moreover, the identified proteins are post-translationally modified by nitric oxide, transcriptionally co-expressed and annotated to function in hydrogen peroxide signaling and the defence response. The activity of one of these proteins, GLYGOLATE OXIDASE 1, a photorespiratory enzyme that produces hydrogen peroxide in response toPseudomonas, was shownAbstract Background Cyclic nucleotides have been shown to play important signaling roles in many physiological processes in plants including photosynthesis and defence. Despite this, little is known about cyclic nucleotide-dependent signaling mechanisms in plants since the downstream target proteins remain unknown. This is largely due to the fact that bioinformatics searches fail to identify plant homologs of protein kinases and phosphodiesterases that are the main targets of cyclic nucleotides in animals. Methods An affinity purification technique was used to identify cyclic nucleotide binding proteins inArabidopsis thaliana . The identified proteins were subjected to a computational analysis that included a sequence, transcriptional co-expression and functional annotation analysis in order to assess their potential role in plant cyclic nucleotide signaling. Results A total of twelve cyclic nucleotide binding proteins were identified experimentally including key enzymes in the Calvin cycle and photorespiration pathway. Importantly, eight of the twelve proteins were shown to contain putative cyclic nucleotide binding domains. Moreover, the identified proteins are post-translationally modified by nitric oxide, transcriptionally co-expressed and annotated to function in hydrogen peroxide signaling and the defence response. The activity of one of these proteins, GLYGOLATE OXIDASE 1, a photorespiratory enzyme that produces hydrogen peroxide in response toPseudomonas, was shown to be repressed by a combination of cGMP and nitric oxide treatment. Conclusions We propose that the identified proteins function together as points of cross-talk between cyclic nucleotide, nitric oxide and reactive oxygen species signaling during the defence response. … (more)
- Is Part Of:
- Cell communication and signaling. Volume 14:Issue 1(2016)
- Journal:
- Cell communication and signaling
- Issue:
- Volume 14:Issue 1(2016)
- Issue Display:
- Volume 14, Issue 1 (2016)
- Year:
- 2016
- Volume:
- 14
- Issue:
- 1
- Issue Sort Value:
- 2016-0014-0001-0000
- Page Start:
- 1
- Page End:
- 18
- Publication Date:
- 2016-12
- Subjects:
- cAMP -- cGMP -- Cross-talk -- Cyclic nucleotide -- Defence response -- H2O2 -- Hypersensitive response -- Nitric oxide -- Reactive oxygen species -- Second messenger
Cell interaction -- Periodicals
571.6 - Journal URLs:
- http://www.biosignaling.com/ ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=221 ↗
http://link.springer.com/ ↗ - DOI:
- 10.1186/s12964-016-0133-2 ↗
- Languages:
- English
- ISSNs:
- 1478-811X
- 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:
- 10061.xml