Volume 2 Issue 1
Jan.  2011
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Qingfeng Chen, Quan Wang, Lizhong Xiong, Zhiyong Lou. A structural view of the conserved domain of rice stress-responsive NAC1[J]. Protein&Cell, 2011, 2(1): 55-63. doi: 10.1007/s13238-011-1010-9
Citation: Qingfeng Chen, Quan Wang, Lizhong Xiong, Zhiyong Lou. A structural view of the conserved domain of rice stress-responsive NAC1[J]. Protein&Cell, 2011, 2(1): 55-63. doi: 10.1007/s13238-011-1010-9

A structural view of the conserved domain of rice stress-responsive NAC1

doi: 10.1007/s13238-011-1010-9
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This work was supported by the National Natural Science Foundation of China (Grant Nos. 30730022 and 30870486), the National Basic Research Program (973 Program) (Grant No. 2007CB914304), and the National Major Projects (grant Nos. 2009ZX09311-001 and 2009ZX10004-304).

  • Received Date: 2011-01-01
  • Rev Recd Date: 2011-01-20
  • The importance of NAC (named as NAM, ATAF1, 2, and CUC2) proteins in plant development, transcription regulation and regulatory pathways involving proteinprotein interactions has been increasingly recognized. We report here the high resolution crystal structure of SNAC1 (stress-responsive NAC) NAC domain at 2.5 Å. Although the structure of the SNAC1 NAC domain shares a structural similarity with the reported structure of the ANAC NAC1 domain, some key features, especially relating to two loop regions which potentially take the responsibility for DNA-binding, distinguish the SNAC1 NAC domain from other reported NAC structures. Moreover, the dimerization of the SNAC1 NAC domain is demonstrated by both soluble and crystalline conditions, suggesting this dimeric state should be conserved in this type of NAC family. Additionally, we discuss the possible NAC-DNA binding model according to the structure and reported biological evidences.
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      沈阳化工大学材料科学与工程学院 沈阳 110142

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