Abstract：
:Auxin is a plant hormone that is central to plant growth and development from embryogenesis to senescence. Auxin signaling is mediated by auxin response transcription factors (ARFs) and Aux/IAA repressors that regulate the expression of a multitude of auxin response genes. ARF and Aux/IAA proteins assemble into homomeric and heteromeric complexes via their conserved PB1 domains. Here we report the first crystal structure of the PB1 complex between ARF5 and IAA17 of Arabidopsis thaliana, which represents the transcriptionally repressed state at low auxin levels. The PB1 domains assemble in a head-to-tail manner with a backbone arrangement similar to that of the ARF5:ARF5 PB1 complex. The ARF5:IAA17 complex, however, reveals distinct points of contact that promote the ARF5:IAA17 interaction over the ARF5:ARF5 interaction. Specifically, surface charges at the interface form salt-bridges that distinguish the homomeric and heteromeric complexes, revealing common and specific interfaces between transcriptionally repressed and derepressed states. Further, the salt-bridges can be reconfigured to switch the affinity between homomeric and heteromeric complexes in an incremental manner. The complex structure combined with quantitative binding analyses would be essential for deciphering the PB1 interaction code underlying the transcriptional regulation of auxin signaling.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Kim Y,Park C,Cha S,Han M,Ryu KS,Suh JYdoi
10.1016/j.jmb.2020.04.007subject
Has Abstractpub_date
2020-06-26 00:00:00pages
4010-4022issue
14eissn
0022-2836issn
1089-8638pii
S0022-2836(20)30285-0journal_volume
432pub_type
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