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A novel extended family of stromal thioredoxins

Cain, Peter, Hall, Michael, Schröder, Wolfgang P., Kieselbach, Thomas, Robinson, Colin (2009) A novel extended family of stromal thioredoxins. Plant Molecular Biology, 70 (3). pp. 273-281. ISSN 0167-4412. (doi:10.1007/s11103-009-9471-4) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:34852)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1007/s11103-009-9471-4

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1007/s11103-009-9471-4
Uncontrolled keywords: Arabidopsis thaliana Chloroplast Protein targeting Subcellular location Thioredoxin
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Colin Robinson
Date Deposited: 24 Jul 2013 15:44 UTC
Last Modified: 16 Nov 2021 10:12 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34852 (The current URI for this page, for reference purposes)

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