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A novel thiol-reductase activity of Arabidopsis YUC6 confers drought tolerance independently of auxin biosynthesis.
Cha, Joon-Yung; Kim, Woe-Yeon; Kang, Sun Bin; Kim, Jeong Im; Baek, Dongwon; Jung, In Jung; Kim, Mi Ri; Li, Ning; Kim, Hyun-Jin; Nakajima, Masatoshi; Asami, Tadao; Sabir, Jamal S M; Park, Hyeong Cheol; Lee, Sang Yeol; Bohnert, Hans J; Bressan, Ray A; Pardo, Jose M; Yun, Dae-Jin.
Afiliación
  • Cha JY; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Kim WY; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Kang SB; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Kim JI; Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
  • Baek D; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Jung IJ; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Kim MR; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Li N; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Kim HJ; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Nakajima M; Department of Applied Biological Chemistry, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
  • Asami T; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Kawaguchi, Saitama 332-0012, Japan.
  • Sabir JS; Department of Applied Biological Chemistry, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
  • Park HC; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Kawaguchi, Saitama 332-0012, Japan.
  • Lee SY; Department of Biochemistry, King Abdulaziz University, Jeddah 21589, Kingdom of Saudi Arabia.
  • Bohnert HJ; Biotechnology Research Group, Department of Biological Science, Faculty of Science, King Abdulaziz University, Jeddah 21589, Kingdom of Saudi Arabia.
  • Bressan RA; Department of Ecological Adaptation, National Institute of Ecology, Seocheon 325-813, Republic of Korea.
  • Pardo JM; Division of Applied Life Science (BK21Plus), PMBBRC &IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea.
  • Yun DJ; Biotechnology Research Group, Department of Biological Science, Faculty of Science, King Abdulaziz University, Jeddah 21589, Kingdom of Saudi Arabia.
Nat Commun ; 6: 8041, 2015 Aug 28.
Article en En | MEDLINE | ID: mdl-26314500
ABSTRACT
YUCCA (YUC) proteins constitute a family of flavin monooxygenases (FMOs), with an important role in auxin (IAA) biosynthesis. Here we report that Arabidopsis plants overexpressing YUC6 display enhanced IAA-related phenotypes and exhibit improved drought stress tolerance, low rate of water loss and controlled ROS accumulation under drought and oxidative stresses. Co-overexpression of an IAA-conjugating enzyme reduces IAA levels but drought stress tolerance is unaffected, indicating that the stress-related phenotype is not based on IAA overproduction. YUC6 contains a previously unrecognized FAD- and NADPH-dependent thiol-reductase activity (TR) that overlaps with the FMO domain involved in IAA biosynthesis. Mutation of a conserved cysteine residue (Cys-85) preserves FMO but suppresses TR activity and stress tolerance, whereas mutating the FAD- and NADPH-binding sites, that are common to TR and FMO domains, abolishes all outputs. We provide a paradigm for a single protein playing a dual role, regulating plant development and conveying stress defence responses.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Asunto principal: Oxidorreductasas / Estrés Fisiológico / Compuestos de Sulfhidrilo / Adaptación Fisiológica / Especies Reactivas de Oxígeno / Estrés Oxidativo / Proteínas de Arabidopsis / Sequías / Oxigenasas de Función Mixta / Ácidos Indolacéticos Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2015 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Asunto principal: Oxidorreductasas / Estrés Fisiológico / Compuestos de Sulfhidrilo / Adaptación Fisiológica / Especies Reactivas de Oxígeno / Estrés Oxidativo / Proteínas de Arabidopsis / Sequías / Oxigenasas de Función Mixta / Ácidos Indolacéticos Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2015 Tipo del documento: Article