Abstract
Environmental stress conditions such as high light, extreme temperatures, salinity or drought trigger oxidative stress and eventually protein misfolding in plants. In chloroplasts, chaperone systems refold proteins after stress, while proteases degrade misfolded and aggregated proteins that cannot be refolded. We observed that reduced activity of chloroplast Hsp70 chaperone or Clp protease systems both prevented growth of Arabidopsis thaliana seedlings after treatment with the oxidative agent methyl viologen. Besides showing a role for these particular protein quality control components on the protection against oxidative stress, we provide evidence supporting the existence of a yet undiscovered pathway for Clp-mediated degradation of the damaged proteins.
Item Type: | Journal article |
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Faculties: | Biology > Department Biology I |
Subjects: | 500 Science > 570 Life sciences; biology |
ISSN: | 1559-2316 |
Language: | English |
Item ID: | 55940 |
Date Deposited: | 14. Jun 2018, 10:00 |
Last Modified: | 04. Nov 2020, 13:36 |