Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2018136 | Plant Science | 2008 | 8 Pages |
Abstract
By the same token, the recent finding of oxidative protein folding in chloroplasts implies an involvement of an enzymatic system for disulfide formation. Mechanisms for oxidative folding in prokaryotes and eukaryotes share a common design, comprising of a thiol oxidase and an oxidative-type thioredoxin such as protein disulfide isomerase. While the localization of protein disulfide isomerases to chloroplasts seems well established, the identity of a chloroplast thiol oxidase is yet to be determined. The understanding of disulfide formation in chloroplasts should prove key to our understanding of redox signaling in general.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Gal Wittenberg, Avihai Danon,