ArticlePlant signaling & behavior2011
Electrophoretic mobility shift assay reveals a novel recognition sequence for Setaria italica NAC protein.
Article in Plant signaling & behavior, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Hello darkness, my old friend: 3-KETOACYL-COENZYME A SYNTHASE4 is a branch point in the regulation of triacylglycerol synthesis in Arabidopsis thaliana.The Plant cell · 2023Article
- Identification of WRKY transcription factor family genes in Pinus massoniana Lamb. and their expression patterns and functions in response to drought stress.BMC plant biology · 2022Article
- NAC transcription factor JUNGBRUNNEN1 enhances drought tolerance in tomato.Plant biotechnology journal · 2018Article
- Genome-Wide Identification and Expression Analysis of the NAC Transcription Factor Family in Cassava.PloS one · 2015Article
- Advances in Setaria genomics for genetic improvement of cereals and bioenergy grasses.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2015Review
- Overexpression of NAC gene from Lepidium latifolium L. enhances biomass, shortens life cycle and induces cold stress tolerance in tobacco: potential for engineering fourth generation biofuel crops.Molecular biology reports · 2014Article
- Genome-wide investigation and expression analyses of WD40 protein family in the model plant foxtail millet (Setaria italica L.).PloS one · 2014Article
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NAC (NAM/ATAF1,2/CUC2) proteins are among the largest family of plant transcription factors. Its members have been associated with diverse plant processes and intricately regulate the expression of several genes. Inspite of this immense progress, knowledge of their DNA-binding properties are still limited. In our recent publication,1 we reported isolation of a membrane-associated NAC domain protein from Setaria italica (SiNAC). Transactivation analysis revealed that it was a functionally active transcription factor as it could stimulate expression of reporter genes in vivo. Truncations of the transmembrane region of the protein lead to its nuclear localization. Here we describe expression and purification of SiNAC DNA-binding domain. We further report identification of a novel DNA-binding site, [C/G][A/T][T/A][G/C]TC[C/G][A/T][C/G][G/C] for SiNAC by electrophoretic mobility shift assay. The SiNAC-GST protein could bind to the NAC recognition sequence in vitro as well as to sequences where some bases had been reshuffled. The results presented here contribute to our understanding of the DNA-binding specificity of SiNAC protein.
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