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Plant and Cell Physiology, 2002, Vol. 43, No. 10 1238-1243
© 2002 Oxford University Press

Short Communications

The Active Site of the Thioredoxin-Like Domain of Chloroplast Protein Disulfide Isomerase, RB60, Catalyzes the Redox-Regulated Binding of Chloroplast Poly(A)-Binding Protein, RB47, to the 5' Untranslated Region of psbA mRNA

Jungmook Kim1,2 and Stephen P. Mayfield

Department of Cell Biology and the Skaggs Institute for Chemical Biology, the Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037, U.S.A.

Abstract

RB60, a chloroplast protein disulfide isomerase, modulates the binding of RB47, chloroplast poly(A)-binding protein, to the 5'-UTR of the psbA mRNA using redox potential, allowing for a reversible switch capable of regulating psbA mRNA translation in a light/dark dependent manner. RB60 contains two thioredoxin-like domains with putative catalytic sites of -Cys-Gly-His-Cys- that are presumed to function as active sites for the redox-regulated changes in RNA-binding activity of RB47. To investigate whether these motifs are required for redox-regulated RNA binding, RNA-gel-mobility shift assays were performed with RB47 and mutant RB60 proteins with single cysteines changed to serines in the -Cys-Gly-His-Cys- motif. The results showed that each thioredoxin-like domain has independent catalytic function in the reactivation of RB47 binding and that a double active site mutant completely lacks the ability to activate RB47 RNA binding activity.

Footnotes

1 Corresponding author: E-mail, jmkim@ksc.kumho.co.kr; Fax, +82-62-972-5085.

2 Present address: Kumho Life and Environmental Science Laboratory, 1 Oryong-Dong, Puk-Gu, Gwangju, Korea 500-712.


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