Thiol-disulfide oxidoreductase PDI1;1 regulates actin structures in Oryza sativa root cells

The polarized and dynamic actin cytoskeleton is essential for root cell growth. Here, we report the key role of thiol-disulfide oxidoreductase PDI1;1 in actin structures. Microscopic analyses revealed that after Oryza sativa roots were exposed to H2O2, both actin and PDI1;1 were depolarized and arranged in a meshwork. In H2O2-exposed cells, actin formed intermolecularly disulfide-bonded high-molecular-weight structures, which were thiol-trapped by PDI1;1. Recombinant PDI1;1 exhibited the ability to recognize actin in an in vitro binding assay. During recovery from H2O2 exposure, the amount of disulfide-bonded high-molecular-weight structures of actin decreased over time, but deficiency of PDI1;1 inhibited the decrease. These results suggest a PDI1;1-dependent pathway that reduces disulfide bonds in high-molecular-weight structures of actin, thus promoting their degradation.