Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites.

ABSTRACT:

Background

Flexibility of plant metabolism is supported by redox regulation of enzymes via posttranslational modification of cysteine residues, especially in plastids. Here, the redox states of cysteine residues are partly coupled to the thioredoxin system and partly to the glutathione pool for reduction. Moreover, several plastid enzymes involved in reactive oxygen species (ROS) scavenging and damage repair draw electrons from glutathione. In addition, cysteine residues can be post-translationally modified by forming a mixed disulfide with glutathione (S-glutathionylation), which protects thiol groups from further oxidation and can influence protein activity. However, the evolution of the plastid glutathione-dependent redox network in land plants and the conservation of cysteine r

SUBMITTER: Muller-Schussele SJ 

PROVIDER: S-EPMC8256493 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature