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PMID: 11034343 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen.

FEBS letters ·Vol. 480 ·No. 2-3 ·2000-09-01 ·Pages 271-6

Kieselbach T, Bystedt M, Hynds P, Robinson C, Schröder WP

Abstract

A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies showed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively. In addition, novel isoforms of PsbO and PsbQ were identified.

MeSH Terms
Amino Acid Sequence Arabidopsis Ascorbate Peroxidases Cell Fractionation Chloroplasts Molecular Sequence Data Peroxidases/analysis,classification Plastocyanin/analysis,classification Proteome/analysis Sequence Homology, Amino Acid Thylakoids/chemistry
Chemicals
Proteome Plastocyanin Peroxidases Ascorbate Peroxidases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kieselbach T
Karolinska Institute, Department of Medical Nutrition, Huddinge, Sweden.
Bystedt M
Hynds P
Robinson C
Schröder W P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2000-09-01
Pages
271-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
Databases
GENBANK
AJ271355
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