Public Release: 

Protein helps plants avoid accumulation of damaged chloroplasts

American Association for the Advancement of Science

The identification of a protein that selectively clears damaged chloroplasts from plant cells reveals how plants maintain a "clean workshop" during the process of photosynthesis. Chloroplasts play an important role in transforming light into useable energy for plants, but when these energy powerhouses are damaged, they release harmful substances. When the plant detects this damage, signals are sent to genes involved in chloroplast function and stress adaptation. Some evidence suggests that plastid ferrochelatases 1 and 2 (FC1 and FC2), enzymes that convert protoporphyrin-IX (Proto) to heme, may play a role in the quality control of individual chloroplasts. Proto is a photosensitizing molecule that generates oxygen, which increases oxidative stress within cells. Jesse Woodson and colleagues therefore created two strains of mutant plants each lacking one of these enzymes and subjected the plants to varying doses of light to observe changes in their chloroplasts. After being in the dark for prolonged periods of time and then suddenly exposed to light, FC1 mutants and controls were able to green, but the FC2 strain did not. A closer look under the microscope revealed this strain had damaged chloroplasts. As well, there was accumulation of Proto and consequently an increased amount of oxygen and expression of oxidative stress responsive genes. The team then searched for additional mutations within the FC2 strain that could counter this effect, identifying Plant U-Box 4 (PUB4) E3 ubiquitin ligase, a regulatory protein involved in cell death and development. Tests of FC2 mutants that also had the PUB4 mutation revealed accumulated Proto and oxygen, but no degradation of the plants' chloroplasts, indicating that PUB4 plays a direct role in signaling chloroplast degradation. Looking closer at healthy plants, the researchers found that PUB4 plays a selective role in chloroplast quality control, further highlighting the function of this protein in reducing oxidative stress.

###

Article #12: "Ubiquitin facilitates a quality-control pathway that removes damaged chloroplasts," by J.D. Woodson; M.S. Joens; A.B. Sinson; J. Gilkerson; J.A. Fitzpatrick; J. Chory at The Salk Institute in La Jolla, CA; A.B. Sinson at University of California, San Diego in La Jolla, CA; J. Gilkerson at Howard Hughes Medical Institute in La Jolla, CA; P.A. Salomé; D. Weigel at Max Planck Institute for Developmental Biology in Tübingen, Germany; M.S. Joens; J.A. Fitzpatrick at Washington University School of Medicine in St. Louis, MO; J. Gilkerson at Shepherd University in Shepherdstown, WV; P.A. Salomé at University of California, Los Angeles in Los Angeles, CA.

Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.