NAC transcription factor: Difference between revisions

Additionally, the NAC domain also modulates protein binding that may determine fate and function of the NAC protein [11-13]. Especially for VNDs, the VNI can directly interact with VND7, and as such, VND7 can directly interact with VND1-5 [13,14]  Such contacts may also be crucial for plant–pathogen interaction or stress tolerance [15,16]. The D subunit of some NAC domains contains a highly hydrophobic negative regulatory domain which acts to suppress transcriptional activity [17]. Many transcription factor family including Dof, WRKY, and APETALA, can be suppressed. Based on my alignment analyses, most of VNDs in Arabidopsis and poplar have this domain, but the function of this domain for VNDs remain elusive. The hydrophobicity associated with 'LVFY' residues or some structual interference with DNA-binding or nuclear transport in this region may be responsible for such repression. Thanks to the prescence of this domain, the positively charged Lys79, the exposed side chain of Arg85, and the hydrogen bond network of Arg 88 may mediate DNA binding activity [17,18]. Furthermore, recent protein structure analyses have shown that NAC domain can change in conformation when binds with DNA [19].