Senescence-associated Barley NAC ( N AM, A TAF1,2, C UC) Transcription Factor Interacts with Radical-induced Cell Death 1 through a Disordered Regulatory Domain *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 286, Issue: 41, Page: 35418-35429
2011
- 81Citations
- 106Captures
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Metrics Details
- Citations81
- Citation Indexes81
- 81
- CrossRef73
- Captures106
- Readers106
- 106
Article Description
Senescence in plants involves massive nutrient relocation and age-related cell death. Characterization of the molecular components, such as transcription factors (TFs), involved in these processes is required to understand senescence. We found that HvNAC005 and HvNAC013 of the plant-specific NAC ( N AM, A TAF1,2, C UC) TF family are up-regulated during senescence in barley ( Hordeum vulgare ). Both Hv NAC005 and Hv NAC013 bound the conserved NAC DNA target sequence. Computational and biophysical analyses showed that both proteins are intrinsically disordered in their large C-terminal domains, which are transcription regulatory domains (TRDs) in many NAC TFs. Using motif searches and interaction studies in yeast we identified an evolutionarily conserved sequence, the LP motif, in the TRD of Hv NAC013. This motif was sufficient for transcriptional activity. In contrast, Hv NAC005 did not function as a transcriptional activator suggesting that an involvement of Hv NAC013 and Hv NAC005 in senescence will be different. Hv NAC013 interacted with barley r adical- i nduced c ell d eath 1 (RCD1) via the very C-terminal part of its TRD, outside of the region containing the LP motif. No significant secondary structure was induced in the Hv NAC013 TRD upon interaction with RCD1. RCD1 also interacted with regions dominated by intrinsic disorder in TFs of the MYB and basic helix-loop-helix families. We propose that RCD1 is a regulatory protein capable of interacting with many different TFs by exploiting their intrinsic disorder. In addition, we present the first structural characterization of NAC C-terminal domains and relate intrinsic disorder and sequence motifs to activity and protein-protein interactions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820737476; http://dx.doi.org/10.1074/jbc.m111.247221; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=80053924427&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/21856750; https://linkinghub.elsevier.com/retrieve/pii/S0021925820737476; http://www.jbc.org/lookup/doi/10.1074/jbc.M111.247221; https://syndication.highwire.org/content/doi/10.1074/jbc.M111.247221; https://dx.doi.org/10.1074/jbc.m111.247221
Elsevier BV
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