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Measuring specific interaction of transcription factor ZmDREB1A with its DNA responsive element at the molecular level

Oxford University Press
Publication Date
  • Nar Methods Online
  • Biology
  • Medicine


OP-NARE120307 9182..9192 A NAC transcription factor and SNI1 cooperatively suppress basal pathogen resistance in Arabidopsis thaliana Ho Soo Kim1,2, Hyeong Cheol Park3, Kyung Eun Kim1,3, Mi Soon Jung3, Hay Ju Han1, Sun Ho Kim3, Young Sang Kwon1, Sunghwa Bahk1, Jonguk An1, Dong Won Bae4, Dae-Jin Yun1,3, Sang-Soo Kwak2 and Woo Sik Chung1,3,* 1Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju 660-701, 2Environmental Biotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 125 Gwahak-ro, Yusong-gu, Daejeon 305-806, 3Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701 and 4Central Instrument Facility, Gyeongsang National University, Jinju 660-701, Korea Received April 13, 2012; Revised and Accepted June 20, 2012 ABSTRACT Transcriptional repression of pathogen defense- related genes is essential for plant growth and de- velopment. Several proteins are known to be involved in the transcriptional regulation of plant defense responses. However, mechanisms by which expression of defense-related genes are regulated by repressor proteins are poorly chara- cterized. Here, we describe the in planta function of CBNAC, a calmodulin-regulated NAC transcrip- tional repressor in Arabidopsis. A T-DNA insertional mutant (cbnac1) displayed enhanced resistance to a virulent strain of the bacterial pathogen Pseudomonas syringae DC3000 (PstDC3000), whereas resistance was reduced in transgenic CBNAC overexpression lines. The observed changes in disease resistance were correlated with alterations in pathogenesis-related protein 1 (PR1) gene expression. CBNAC bound directly to the PR1 promoter. SNI1 (suppressor of nonexpressor of PR genes1, inducible 1) was identified as a CBNAC- binding protein. Basal resistance to PstDC3000 and derepression of PR1 expression was greater in the cbnac1 sni1 double mutant than in either cbnac1 or sni1 mutants. SNI1 enhanced binding of CBNAC to its co

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