T. Kieselbach et al., A peroxidase homologue and novel plastocyanin located by proteomics to theArabidopsis chloroplast thylakoid lumen, FEBS LETTER, 480(2-3), 2000, pp. 271-276
A study by two-dimensional electrophoresis showed that the soluble, lumenal
fraction of Arabidopsis thaliana thylakoids can be resolved into 300 prote
in spots. After subtraction of low-intensity spots and accounting for low-l
evel stromal contamination, the number of more abundant, lumenal proteins w
as estimated to be between 30 and 60. Two of these proteins have been ident
ified: a novel plastocyanin that also was the predominant component of the
total plastocyanin pool, and a putative ascorbate peroxidase. Import studie
s shamed that these proteins are routed to the thylakoid lumen by the Sec-
and delta pH-dependent translocation pathways, respectively, In addition, n
ovel isoforms of PsbO and PsbQ were identified, (C) 2000 Federation of Euro
pean Biochemical Societies. Published by Elsevier Science B.V. All rights r
eserved.