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The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature
Södertörn University, School of Life Sciences. Karolinska Institute.
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2006 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 47, no 5, 720-734 p.Article in journal (Refereed) Published
Abstract [en]

Cold acclimation and over-wintering by herbaceous plants are energetically expensive and are dependent on functional plastid metabolism. To understand how the stroma and the lumen proteomes adapt to low temperatures, we have taken a proteomic approach (difference gel electrophoresis) to identify proteins that changed in abundance in Arabidopsis chloroplasts during cold shock (1 day), and short- (10 days) and long-term (40 days) acclimation to 5 degrees C. We show that cold shock (1 day) results in minimal change in the plastid proteomes, while short-term (10 days) acclimation results in major changes in the stromal but few changes in the lumen proteome. Long-term acclimation (40 days) results in modulation of the proteomes of both compartments, with new proteins appearing in the lumen and further modulations in protein abundance occurring in the stroma. We identify 43 differentially displayed proteins that participate in photosynthesis, other plastid metabolic functions, hormone biosynthesis and stress sensing and signal transduction. These findings not only provide new insights into the cold response and acclimation of Arabidopsis, but also demonstrate the importance of studying changes in protein abundance within the relevant cellular compartment.

Place, publisher, year, edition, pages
2006. Vol. 47, no 5, 720-734 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:sh:diva-14282DOI: 10.1111/j.1365-313X.2006.02821.xISI: 000239700000006PubMedID: 16923014ScopusID: 2-s2.0-33747046042OAI: oai:DiVA.org:sh-14282DiVA: diva2:468674
Available from: 2011-12-21 Created: 2011-12-20 Last updated: 2014-03-17Bibliographically approved

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Schubert, Maria
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