4dul
ANAC019 NAC domain crystal form IVANAC019 NAC domain crystal form IV
Structural highlights
Publication Abstract from PubMedNAC (NAM/ATAF/CUC) plant transcription factors regulate essential processes in development, stress responses and nutrient distribution in important crop and model plants (rice, Populus, Arabidopsis), which makes them highly relevant in the context of crop optimization and bioenergy production. The structure of the DNA-binding NAC domain of ANAC019 has previously been determined by X-ray crystallography, revealing a dimeric and predominantly beta-fold structure, but the mode of binding to cognate DNA has remained elusive. In this study, information from low resolution X-ray structures and small angle X-ray scattering on complexes with oligonucleotides, mutagenesis and (DNaseI and uranyl photo-) footprinting, is combined to form a structural view of DNA-binding, and for the first time provide experimental evidence for the speculated relationship between plant specific NAC proteins, WRKY transcription factors and the mammalian GCM transcription factors, which all use a b-strand motif for DNA-binding. The structure shows how the NAC domain inserts the edge of its core beta-sheet in the major groove, while leaving the DNA largely un-distorted. The structure of the NAC-DNA complex and a new crystal form of the unbound NAC also indicate limited flexibility of the NAC dimer arrangement which could be important in recognizing suboptimal binding sites. DNA binding by the plant specific NAC transcription factors in crystal and solution: a firm link to WRKY and GCM transcription factors.,Welner DH, Lindemose S, Grossmann JG, Mollegaard NE, Olsen AN, Helgstrand C, Skriver K, Lo Leggio L Biochem J. 2012 Mar 29. PMID:22455904[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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