7xp3
DNA complex form of ORESARA1(ANAC092) NAC DomainDNA complex form of ORESARA1(ANAC092) NAC Domain
Structural highlights
FunctionNAC92_ARATH Transcription activator that binds to DNA in promoters of target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5-6n)[CT]AC[AG]-3' (PubMed:23340744). Promotes lateral root development (PubMed:16359384). Triggers the expression of senescence-associated genes during age-, salt- and dark-induced senescence through a regulatory network that may involve cross-talk with salt- and H(2)O(2)-dependent signaling pathways (PubMed:15295076, PubMed:20113437, PubMed:21303842, PubMed:9351240). Also regulates genes during seed germination (PubMed:20113437). Positively regulates aging-induced cell death (PubMed:19229035). Involved in age-related resistance (ARR) against Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis (PubMed:19694953). Antagonizes GLK1 and GLK2 transcriptional activity, shifting the balance from chloroplast maintenance towards deterioration during leaf senescence (PubMed:23459204). Promotes the expression of senescence-associated genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during senescence onset (PubMed:23340744).[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedPlants use sophisticated mechanisms of gene expression to control senescence in response to environmental stress or aging. ORE1 (Arabidopsis thaliana NAC092) is a master regulator of senescence that belongs to the plant-specific NAC transcription factor protein family. ORE1 has been reported to bind to multiple DNA targets to orchestrate leaf senescence, yet the mechanistic basis for recognition of the cognate gene sequence remains unclear. Here, we report the crystal structure of the ORE1-NAC domain alone and its DNA-binding form. The structure of DNA-bound ORE1-NAC revealed the molecular basis for nucleobase recognition and phosphate backbone interactions. We show that local versatility in the DNA-binding site, in combination with domain flexibility of the ORE-NAC homodimer, is crucial for the maintenance of binding to intrinsically flexible DNA. Our results provide a platform for understanding other plant-specific NAC protein-DNA interactions as well as insight into the structural basis of NAC regulators in plants of agronomic and scientific importance. Structural basis of DNA binding by the NAC transcription factor ORE1, a master regulator of plant senescence.,Chun I, Kim HJ, Hong S, Kim YG, Kim MS Plant Commun. 2023 May 8;4(3):100510. doi: 10.1016/j.xplc.2022.100510. Epub 2022 , Dec 23. PMID:36564947[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|