Abstract
Plants need light energy to drive photosynthesis, but excess energy leads to the production of harmful reactive oxygen species (ROS), resulting in oxidative inactivation of target enzymes, including the photosynthetic CO2-fixing enzyme, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). It has been demonstrated in vitro that oxidatively inactivated Rubisco can be reactivated by the addition of reducing agents. Busch et al. (in The Plant Journal, doi: 10.1111/tpj.14617, 2020) recently demonstrated that bundle-sheath defective 2 (BSD2), a stroma-targeted protein formerly known as a late-assembly chaperone for Rubisco biosynthesis, can be responsible for such reactivation in vivo. Here, we propose a working model of the novel redox regulation in Rubisco activity. Redox of Rubisco may be a new target for improving photosynthesis.
Keywords:
Photosynthesis; ROS; chloroplast; disulfide bond; recovery; stress; thiol.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Arabidopsis / metabolism*
-
Arabidopsis Proteins / chemistry
-
Arabidopsis Proteins / metabolism*
-
Chloroplast Proteins / chemistry
-
Chloroplast Proteins / metabolism*
-
Chloroplasts / metabolism
-
Molecular Chaperones / chemistry
-
Molecular Chaperones / metabolism*
-
Oxidation-Reduction
-
Ribulose-Bisphosphate Carboxylase / physiology*
-
Zinc Fingers
Substances
-
AT3G47650 protein, Arabidopsis
-
Arabidopsis Proteins
-
Chloroplast Proteins
-
Molecular Chaperones
-
Ribulose-Bisphosphate Carboxylase
Grants and funding
This work was supported in part by JSPS KAKENHI Grant Numbers 26450081 (H.S.) and 18J00308 (J.T.), A-STEP from the Japan Science and Technology Agency (H.S.), grants from the Advanced Low Carbon Technology Research and Development Program from the Japan Science and Technology Agency (S.T. and H.S.). J.T. is supported by Research Fellowships for Young Scientists from JSPS.