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A novel extended family of stromal thioredoxins
Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK .
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
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2009 (English)In: Plant Molecular Biology, ISSN 0167-4412, E-ISSN 1573-5028, Vol. 70, no 3, 273-281 p.Article in journal (Refereed) Published
Abstract [en]

Thioredoxins play key regulatory roles in chloroplasts by linking photosynthetic light reactions to a series of plastid functions. In addition to the established groups of thioredoxins, f, m, x, and y, novel plant thioredoxins were also considered to include WCRKC motif proteins, CDSP32, the APR proteins, the lilium proteins and HCF164. Despite their important roles, the subcellular locations of many novel thioredoxins has remained unknown. Here, we report a study of their subcellular location using the cDNA clone resources of TAIR. In addition to filling all gaps in the subcellular map of the established chloroplast thioredoxins f, m, x and y, we show that the members of the WCRKC family are targeted to the stroma and provide evidence for a stromal location of the lilium proteins. The combined data from this and related studies indicate a consistent stromal location of the known Arabidopsis chloroplast thioredoxins except for thylakoid-bound HCF164.

Place, publisher, year, edition, pages
SpringerLink , 2009. Vol. 70, no 3, 273-281 p.
Keyword [en]
Arabidopsis thaliana, Chloroplast, Protein targeting, Subcellular location, Thioredoxin
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-19625DOI: 10.1007/s11103-009-9471-4PubMedID: 19259774OAI: oai:DiVA.org:umu-19625DiVA: diva2:202184
Available from: 2009-03-09 Created: 2009-03-09 Last updated: 2017-12-13Bibliographically approved
In thesis
1. The chloroplast lumen: New insights into thiol redox regulation and functions of lumenal proteins
Open this publication in new window or tab >>The chloroplast lumen: New insights into thiol redox regulation and functions of lumenal proteins
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In higher plants oxygenic photosynthesis primarily takes place in the chloroplasts of leaves. Within the chloroplasts is an intricate membrane system, the thylakoid membrane, which is the site of light harvesting and photosynthetic electron transport. Enclosed by this membrane is the lumen space, which initially was believed to only contain a few proteins, but now is known to house a distinct set of >50 proteins, many for which there is still no proposed function. The work presented in this thesis is focused on understanding the functions of the proteins in the lumen space. Using proteomic methods, we investigated first the regulation of lumenal proteins by light and secondly by dithiol-disulphide exchange, mediated by the disulphide reductase protein thioredoxin. We furthermore performed structural and functional studies of the lumenal pentapeptide repeat proteins and of the PsbP-domain protein PPD6. When studying the diurnal expression pattern of the lumen proteins, using difference gel electrophoresis, we observed an increased abundance of fifteen lumen protein in light-adapted Arabidopsis thaliana plants. Among these proteins were subunits of the oxygen evolving complex, plastocyanin and proteins of unknown function. In our analysis of putative lumenal targets of thioredoxin, we identified nineteen proteins, constituting more than 40 % of the lumen proteins observable by our methods. A subset of these putative target proteins were selected for further studies, including structure determination by x-ray crystallography. The crystal structure of the pentapeptide repeat protein TL15 was solved to 1.3 Å resolution and further biochemical characterization suggested that it may function as a novel type of redox regulated molecular chaperone in the lumen. PPD6, a member of the PsbP-family of proteins, which is unique in that it possesses a conserved disulphide bond not found in any other PsbP-family protein, was also expressed, purified and crystallized. A preliminary x-ray analysis suggests that PPD6 exists as a dimer in the crystalline state and binds zinc ions. The high representation of targets of thioredoxin among the lumen proteins, along with the characterization of the pentapeptide repeat protein family, implies that dithiol-disulphide exchange reactions play an important role in the thylakoid lumen of higher plants, regulating processes such as photoprotection, protein turnover and protein folding.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2012. 65 p.
Keyword
Photosynthesis, thylakoid lumen, thioredoxin, pentapeptide repeat, proteomics
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-58423 (URN)978-91-7459-467-6 (ISBN)
Public defence
2012-09-21, KBC huset, KB3B1, Umeå Universitet, Umeå, 09:00 (English)
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Available from: 2012-08-31 Created: 2012-08-29 Last updated: 2012-08-30Bibliographically approved

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