FAD and NADPH binding sites of YUCCA6 are essential for chaperone activity and oxidative stress tolerance in Arabidopsis thaliana.

Autor: Ahn G; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Jeong SY; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Khan HA; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Aulia AC; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Shin GI; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Ji MG; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Sultana Chowdhury MS; College of Pharmacy, Yeungnam University, Gyeongsan, 38541, Republic of Korea., Kim DY; College of Pharmacy, Yeungnam University, Gyeongsan, 38541, Republic of Korea., Lee SY; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea., Yun DJ; Department of Biomedical Science and Engineering, Konkuk University, Seoul, 05029, Republic of Korea., Kim WY; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea. Electronic address: kim1312@gnu.ac.kr., Cha JY; Division of Applied Life Science (BK21four), PBRRC, IALS, and RILS, Gyeongsang National University, Jinju, 52828, Republic of Korea. Electronic address: jycha@gnu.ac.kr.
Jazyk: angličtina
Zdroj: Plant physiology and biochemistry : PPB [Plant Physiol Biochem] 2025 Jan; Vol. 218, pp. 109335. Date of Electronic Publication: 2024 Nov 26.
DOI: 10.1016/j.plaphy.2024.109335
Abstrakt: Phytohormone auxin plays a pivotal role in governing plant growth, development, and responses to abiotic stresses. YUCCA6 (YUC6), an auxin biosynthetic enzyme belonging to the flavin monooxygenase (FMO) subfamily, converts indole-3-pyruvic acid to indole-3-acetic acid. Our prior investigation uncovered that YUC6 also functions as a thiol-reductase and chaperone in a Cys85-dependent manner, resulting in conferred tolerance to nickel heavy metal stress and drought and delayed leaf senescence. Notably, the conserved co-factor binding sites (FAD and NADPH) in YUC6, shared with FMOs and thioredoxin reductase, prompted our exploration into their significance for holdase chaperone activity and oxidative stress tolerance in Arabidopsis. We demonstrate that YUC6 transcripts are upregulated in response to methyl viologen (MV)-induced oxidative stress, implicating YUC6 in oxidative stress response. Mutations in co-factor binding sites markedly diminish the chaperone activity of YUC6, and reduce the YUC6-mediated oxidative stress tolerance in Arabidopsis. Furthermore, YUC6 proteins exist as oligomeric states under native conditions, formed by disulfide-bond bridges. Oligomeric YUC6 displays enhanced chaperone activity compared to its monomeric YUC6. We found here that co-factor binding sites of YUC6 are necessary for its chaperone properties.
Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest.
(Copyright © 2024 Elsevier Masson SAS. All rights reserved.)
Databáze: MEDLINE
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