Functional characterization of Ostreococcus tauri phototropin. Issue 2 (28th September 2015)
- Record Type:
- Journal Article
- Title:
- Functional characterization of Ostreococcus tauri phototropin. Issue 2 (28th September 2015)
- Main Title:
- Functional characterization of Ostreococcus tauri phototropin
- Authors:
- Sullivan, Stuart
Petersen, Jan
Blackwood, Lisa
Papanatsiou, Maria
Christie, John M. - Abstract:
- Summary: Phototropins (phots) regulate a range of adaptive processes in plants that serve to optimize photosynthetic efficiency and promote growth. Light sensing by Arabidopsis thaliana phots is predominantly mediated by the Light, Oxygen and Voltage sensing 2 (LOV2) flavin‐binding motif located within the N‐terminus of the photoreceptor. Here we characterize the photochemical and biochemical properties of phot from the marine picoalga Ostreococcus tauri phototropin (Otphot) and examine its ability to replace phot‐mediated function in Arabidopsis . Photochemical properties of Otphot rely on both LOV1 and LOV2. Yet, biochemical analysis indicates that light‐dependent receptor autophosphorylation is primarily dependent on LOV2. As found for Arabidopsis phots, Otphot associates with the plasma membrane and partially internalizes, albeit to a limited extent, in response to blue‐light irradiation. Otphot is able to elicit a number of phot‐regulated processes in Arabidopsis, including petiole positioning, leaf expansion, stomatal opening and chloroplast accumulation movement. However, Otphot is unable to restore phototropism and chloroplast avoidance movement. Consistent with its lack of phototropic function in Arabidopsis, Otphot does not associate with or trigger dephosphorylation of the phototropic signalling component Non‐Phototropic Hypocotyl 3 (NPH3). Taken together, these findings indicate that the mechanism of action of plant and evolutionarily distant algal phots is lessSummary: Phototropins (phots) regulate a range of adaptive processes in plants that serve to optimize photosynthetic efficiency and promote growth. Light sensing by Arabidopsis thaliana phots is predominantly mediated by the Light, Oxygen and Voltage sensing 2 (LOV2) flavin‐binding motif located within the N‐terminus of the photoreceptor. Here we characterize the photochemical and biochemical properties of phot from the marine picoalga Ostreococcus tauri phototropin (Otphot) and examine its ability to replace phot‐mediated function in Arabidopsis . Photochemical properties of Otphot rely on both LOV1 and LOV2. Yet, biochemical analysis indicates that light‐dependent receptor autophosphorylation is primarily dependent on LOV2. As found for Arabidopsis phots, Otphot associates with the plasma membrane and partially internalizes, albeit to a limited extent, in response to blue‐light irradiation. Otphot is able to elicit a number of phot‐regulated processes in Arabidopsis, including petiole positioning, leaf expansion, stomatal opening and chloroplast accumulation movement. However, Otphot is unable to restore phototropism and chloroplast avoidance movement. Consistent with its lack of phototropic function in Arabidopsis, Otphot does not associate with or trigger dephosphorylation of the phototropic signalling component Non‐Phototropic Hypocotyl 3 (NPH3). Taken together, these findings indicate that the mechanism of action of plant and evolutionarily distant algal phots is less well conserved than previously thought. … (more)
- Is Part Of:
- New phytologist. Volume 209:Issue 2(2016)
- Journal:
- New phytologist
- Issue:
- Volume 209:Issue 2(2016)
- Issue Display:
- Volume 209, Issue 2 (2016)
- Year:
- 2016
- Volume:
- 209
- Issue:
- 2
- Issue Sort Value:
- 2016-0209-0002-0000
- Page Start:
- 612
- Page End:
- 623
- Publication Date:
- 2015-09-28
- Subjects:
- Arabidopsis thaliana -- blue light -- flavin -- Ostreococcus tauri -- Light, Oxygen and Voltage (LOV) domain -- phosphorylation -- phototropin
Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.13640 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 22188.xml