CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co‐chaperonin role in Arabidopsis chloroplasts. Issue 1 (11th October 2012)
- Record Type:
- Journal Article
- Title:
- CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co‐chaperonin role in Arabidopsis chloroplasts. Issue 1 (11th October 2012)
- Main Title:
- CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co‐chaperonin role in Arabidopsis chloroplasts
- Authors:
- Kuo, W. Y.
Huang, C. H.
Liu, A. C.
Cheng, C. P.
Li, S. H.
Chang, W. C.
Weiss, C.
Azem, A.
Jinn, T. L. - Abstract:
- <abstract abstract-type="main" xml:lang="en" id="nph4369-abs-0001"> <title>Summary</title> <p> <list id="nph4369-list-0001" list-type="bullet"> <list-item> <p>Iron superoxide dismutases (FeSODs; FSDs) are primary antioxidant enzymes in <italic>Arabidopsis thaliana</italic> chloroplasts. The stromal FSD1 conferred the only detectable FeSOD activity, whereas the thylakoid membrane‐ and nucleoid‐co‐localized FSD2 and FSD3 double mutant showed arrested chloroplast development.</p> </list-item> <list-item> <p>FeSOD requires cofactor Fe for its activity, but its mechanism of activation is unclear. We used reversed‐phase high‐performance liquid chromatography (HPLC), gel filtration chromatography, LC‐MS/MS, protoplast transient expression and virus‐induced gene silencing (VIGS) analyses to identify and characterize a factor involved in FeSOD activation.</p> </list-item> <list-item> <p>We identified the chloroplast‐localized co‐chaperonin CHAPERONIN 20 (CPN20) as a mediator of FeSOD activation by direct interaction. The relationship between CPN20 and FeSOD was confirmed by <italic>in vitro</italic> experiments showing that CPN20 alone could enhance FSD1, FSD2 and FSD3 activity. The <italic>in vivo</italic> results showed that <italic>CPN20‐</italic>overexpressing mutants and mutants with defective co‐chaperonin activity increased FSD1 activity, without changing the chaperonin CPN60 protein level, and VIGS‐induced downregulation of <italic>CPN20</italic> also led to decreased FeSOD<abstract abstract-type="main" xml:lang="en" id="nph4369-abs-0001"> <title>Summary</title> <p> <list id="nph4369-list-0001" list-type="bullet"> <list-item> <p>Iron superoxide dismutases (FeSODs; FSDs) are primary antioxidant enzymes in <italic>Arabidopsis thaliana</italic> chloroplasts. The stromal FSD1 conferred the only detectable FeSOD activity, whereas the thylakoid membrane‐ and nucleoid‐co‐localized FSD2 and FSD3 double mutant showed arrested chloroplast development.</p> </list-item> <list-item> <p>FeSOD requires cofactor Fe for its activity, but its mechanism of activation is unclear. We used reversed‐phase high‐performance liquid chromatography (HPLC), gel filtration chromatography, LC‐MS/MS, protoplast transient expression and virus‐induced gene silencing (VIGS) analyses to identify and characterize a factor involved in FeSOD activation.</p> </list-item> <list-item> <p>We identified the chloroplast‐localized co‐chaperonin CHAPERONIN 20 (CPN20) as a mediator of FeSOD activation by direct interaction. The relationship between CPN20 and FeSOD was confirmed by <italic>in vitro</italic> experiments showing that CPN20 alone could enhance FSD1, FSD2 and FSD3 activity. The <italic>in vivo</italic> results showed that <italic>CPN20‐</italic>overexpressing mutants and mutants with defective co‐chaperonin activity increased FSD1 activity, without changing the chaperonin CPN60 protein level, and VIGS‐induced downregulation of <italic>CPN20</italic> also led to decreased FeSOD activity.</p> </list-item> <list-item> <p>Our findings reveal that CPN20 can mediate FeSOD activation in chloroplasts, a role independent of its known function in the chaperonin system.</p> </list-item> </list> </p> </abstract> … (more)
- Is Part Of:
- New phytologist. Volume 197:Issue 1(2013)
- Journal:
- New phytologist
- Issue:
- Volume 197:Issue 1(2013)
- Issue Display:
- Volume 197, Issue 1 (2013)
- Year:
- 2013
- Volume:
- 197
- Issue:
- 1
- Issue Sort Value:
- 2013-0197-0001-0000
- Page Start:
- 99
- Page End:
- 110
- Publication Date:
- 2012-10-11
- 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/j.1469-8137.2012.04369.x ↗
- 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:
- 4275.xml