AtSIA1 AND AtOSA1: two Abc1 proteins involved in oxidative stress responses and iron distribution within chloroplasts. Issue 2 (4th October 2013)
- Record Type:
- Journal Article
- Title:
- AtSIA1 AND AtOSA1: two Abc1 proteins involved in oxidative stress responses and iron distribution within chloroplasts. Issue 2 (4th October 2013)
- Main Title:
- AtSIA1 AND AtOSA1: two Abc1 proteins involved in oxidative stress responses and iron distribution within chloroplasts
- Authors:
- Manara, Anna
DalCorso, Giovanni
Leister, Dario
Jahns, Peter
Baldan, Barbara
Furini, Antonella - Abstract:
- <abstract abstract-type="main" id="nph12533-abs-0001"> <title>Summary</title> <p> <list id="nph12533-list-0001" list-type="bullet"> <list-item> <p>The Abc1 protein kinases are a large family of functionally diverse proteins with multiple roles in the regulation of respiration and oxidative stress tolerance.</p> </list-item> <list-item> <p>A functional characterization was carried out for AtSIA1, an <italic>Arabidopsis thaliana</italic> Abc1‐like protein, focusing on its potential redundancy with its homolog AtOSA1. Both proteins are located within chloroplasts, even if a different subplastidial localization seems probable. The comparison of <italic>atsia1</italic> and <italic>atosa1</italic> mutants, <italic>atsia1/atosa1</italic> double mutant and wild‐type plants revealed a reduction in plastidial iron‐containing proteins of the Cyt<italic>b</italic><sub><italic>6</italic></sub><italic>f</italic> complex in the mutants. Iron uptake from soil is not hampered in mutant lines, suggesting that AtSIA1 and AtOSA1 affect iron distribution within the chloroplast.</p> </list-item> <list-item> <p>Mutants accumulated more ferritin and superoxide, and showed reduced tolerance to reactive oxygen species (ROS), potentially indicating a basal role in oxidative stress. The mutants produced higher concentrations of plastochromanol and plastoquinones than wild‐type plants, but only <italic>atsia1</italic> plants developed larger plastoglobules and contained higher concentrations of α‐ and<abstract abstract-type="main" id="nph12533-abs-0001"> <title>Summary</title> <p> <list id="nph12533-list-0001" list-type="bullet"> <list-item> <p>The Abc1 protein kinases are a large family of functionally diverse proteins with multiple roles in the regulation of respiration and oxidative stress tolerance.</p> </list-item> <list-item> <p>A functional characterization was carried out for AtSIA1, an <italic>Arabidopsis thaliana</italic> Abc1‐like protein, focusing on its potential redundancy with its homolog AtOSA1. Both proteins are located within chloroplasts, even if a different subplastidial localization seems probable. The comparison of <italic>atsia1</italic> and <italic>atosa1</italic> mutants, <italic>atsia1/atosa1</italic> double mutant and wild‐type plants revealed a reduction in plastidial iron‐containing proteins of the Cyt<italic>b</italic><sub><italic>6</italic></sub><italic>f</italic> complex in the mutants. Iron uptake from soil is not hampered in mutant lines, suggesting that AtSIA1 and AtOSA1 affect iron distribution within the chloroplast.</p> </list-item> <list-item> <p>Mutants accumulated more ferritin and superoxide, and showed reduced tolerance to reactive oxygen species (ROS), potentially indicating a basal role in oxidative stress. The mutants produced higher concentrations of plastochromanol and plastoquinones than wild‐type plants, but only <italic>atsia1</italic> plants developed larger plastoglobules and contained higher concentrations of α‐ and γ‐tocopherol and VTE1.</p> </list-item> <list-item> <p>Taken together, these data suggest that AtSIA1 and AtOSA1 probably act in signaling pathways that influence responses to ROS production and oxidative stress.</p> </list-item> </list> </p> </abstract> … (more)
- Is Part Of:
- New phytologist. Volume 201:Issue 2(2014)
- Journal:
- New phytologist
- Issue:
- Volume 201:Issue 2(2014)
- Issue Display:
- Volume 201, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 201
- Issue:
- 2
- Issue Sort Value:
- 2014-0201-0002-0000
- Page Start:
- 452
- Page End:
- 465
- Publication Date:
- 2013-10-04
- Subjects:
- 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.12533 ↗
- 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:
- 3752.xml