Lon domain‐containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts. Issue 6 (22nd November 2019)

• Record Type: Journal Article
• Authors: Shin, Jin Seok; Kim, Soo Youn; So, Won Mi; Noh, Minsoo; Yoo, Kyoung Shin; Shin, Jeong Sheop
• Is Part Of: FEBS letters. Volume 594:Issue 6(2020)
• Page Start: 986
• Page End: 994
• Publication Date: 2019-11-22
• Subjects: Arabidopsis -- chloroplast -- dehiscence -- lignification -- ROS -- thioredoxin; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13664
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Plant thioredoxins (Trxs) act as antioxidants and function as redox regulators in the chloroplast. Although the regulation of ROS in chloroplasts is well elucidated, the precise regulation mechanism of Trx remains unknown. Here, we characterize a novel chloroplast protein, Lon domain‐containing protein 1 (LCP1), which contains only a Lon domain, the precise function of which is not known. We find that LCP1 interacts with Trx‐y2 and represses its activity, and that knockdown (KD) of LCP1 causes anther indehiscence due to deficient lignin deposition. In addition, LCP1 KD plants show less ROS accumulation and lower expression of ROS‐responsive marker genes than the wild‐type plant. Taken together, we suggest that LCP1 directly regulates Trx‐y2 and controls H2 O2 levels and, thereby, regulates lignin polymerization in the anther endothecium. Abstract :