Thioredoxin targets of the plant chloroplast lumen and their implications for plastid function
(2010) In Proteomics 10(5). p.987-1001- Abstract
- The light-dependent regulation of stromal enzymes by thioredoxin (Trx)-catalysed disulphide/dithiol exchange is known as a classical mechanism for control of chloroplast metabolism. Recent proteome studies show that Trx targets are present not only in the stroma but in all chloroplast compartments, from the envelope to the thylakoid lumen. Trx-mediated redox control appears to be a common feature of important pathways, such as the Calvin cycle, starch synthesis and tetrapyrrole biosynthesis. However, the extent of thiol-dependent redox regulation in the thylakoid lumen has not been previously systematically explored. In this study, we addressed Trx-linked redox control in the chloroplast lumen of Arabidopsis thaliana. Using complementary... (More)
- The light-dependent regulation of stromal enzymes by thioredoxin (Trx)-catalysed disulphide/dithiol exchange is known as a classical mechanism for control of chloroplast metabolism. Recent proteome studies show that Trx targets are present not only in the stroma but in all chloroplast compartments, from the envelope to the thylakoid lumen. Trx-mediated redox control appears to be a common feature of important pathways, such as the Calvin cycle, starch synthesis and tetrapyrrole biosynthesis. However, the extent of thiol-dependent redox regulation in the thylakoid lumen has not been previously systematically explored. In this study, we addressed Trx-linked redox control in the chloroplast lumen of Arabidopsis thaliana. Using complementary proteomics approaches, we identified 19 Trx target proteins, thus covering more than 40% of the currently known lumenal chloroplast proteome. We show that the redox state of thiols is decisive for degradation of the extrinsic PsbO1 and PsbO2 subunits of photosystem II. Moreover, disulphide reduction inhibits activity of the xanthophyll cycle enzyme violaxanthin deepoxidase, which participates in thermal dissipation of excess absorbed light. Our results indicate that redox-controlled reactions in the chloroplast lumen play essential roles in the function of photosystem II and the regulation of adaptation to light intensity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1587268
- author
- Hall, Michael ; Mata-Cabana, Alejandro ; Åkerlund, Hans-Erik LU ; Florencio, Francisco J. ; Schroder, Wolfgang P. ; Lindahl, Marika and Kieselbach, Thomas
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- proteomics, Violaxanthin de-epoxidase, Disulphide, D1-processing, Immunophilin, Plant, Pentapeptide protein
- in
- Proteomics
- volume
- 10
- issue
- 5
- pages
- 987 - 1001
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000275790700009
- scopus:77649126670
- pmid:20049866
- ISSN
- 1615-9861
- DOI
- 10.1002/pmic.200900654
- language
- English
- LU publication?
- yes
- id
- cb74f018-f4b6-4961-9faa-b10fb441e369 (old id 1587268)
- date added to LUP
- 2016-04-01 09:55:23
- date last changed
- 2022-04-12 00:13:02
@article{cb74f018-f4b6-4961-9faa-b10fb441e369,
abstract = {{The light-dependent regulation of stromal enzymes by thioredoxin (Trx)-catalysed disulphide/dithiol exchange is known as a classical mechanism for control of chloroplast metabolism. Recent proteome studies show that Trx targets are present not only in the stroma but in all chloroplast compartments, from the envelope to the thylakoid lumen. Trx-mediated redox control appears to be a common feature of important pathways, such as the Calvin cycle, starch synthesis and tetrapyrrole biosynthesis. However, the extent of thiol-dependent redox regulation in the thylakoid lumen has not been previously systematically explored. In this study, we addressed Trx-linked redox control in the chloroplast lumen of Arabidopsis thaliana. Using complementary proteomics approaches, we identified 19 Trx target proteins, thus covering more than 40% of the currently known lumenal chloroplast proteome. We show that the redox state of thiols is decisive for degradation of the extrinsic PsbO1 and PsbO2 subunits of photosystem II. Moreover, disulphide reduction inhibits activity of the xanthophyll cycle enzyme violaxanthin deepoxidase, which participates in thermal dissipation of excess absorbed light. Our results indicate that redox-controlled reactions in the chloroplast lumen play essential roles in the function of photosystem II and the regulation of adaptation to light intensity.}},
author = {{Hall, Michael and Mata-Cabana, Alejandro and Åkerlund, Hans-Erik and Florencio, Francisco J. and Schroder, Wolfgang P. and Lindahl, Marika and Kieselbach, Thomas}},
issn = {{1615-9861}},
keywords = {{proteomics; Violaxanthin de-epoxidase; Disulphide; D1-processing; Immunophilin; Plant; Pentapeptide protein}},
language = {{eng}},
number = {{5}},
pages = {{987--1001}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Proteomics}},
title = {{Thioredoxin targets of the plant chloroplast lumen and their implications for plastid function}},
url = {{http://dx.doi.org/10.1002/pmic.200900654}},
doi = {{10.1002/pmic.200900654}},
volume = {{10}},
year = {{2010}},
}