Fig. 1: Overall structures of SAP05 bound to TFs and RPN10. | Nature Communications

Fig. 1: Overall structures of SAP05 bound to TFs and RPN10.

From: Molecular basis of SAP05-mediated ubiquitin-independent proteasomal degradation of transcription factors

Fig. 1

a Domain architecture of Arabidopsis thaliana (At) GATA18, AtSPL5, onion yellows phytoplasma (OY-M) SAP05 and AtRPN10. ZnF, zinc finger; SP, signal peptide; vWA, von Willebrand factor A; UIM, ubiquitin-interacting motif. b Superdex 75 Increase 10/300 gel-filtration chromatography profiles of SAP05 alone and in complex with SPL5, RPN10 and both. Left panel, SDS-PAGE gel of the peak fractions, stained with Coomassie blue. Source data are provided as a Source Data file. Representative images, n = 3. c, d ITC measurements of binding affinities (KD) of OY-M SAP05 to AtGATA18 and AtSPL5 ZnF domains, respectively. e Ribbon diagram of the crystal structure of OY-M SAP05-AtGATA18 complex. Zinc ion is shown as a sphere. Four zinc-coordinating cysteine residues of AtGATA18 are numbered and shown in schematic form. f Crystal structure of OY-M SAP05-AtSPL5 complex. AtSPL5 coordinates two non-interleaved Zn1 and Zn2 sites and is separated into an N-terminal subdomain (Nt-sub) and a C-terminal subdomain (Ct-sub). g Crystal structure of OY-M SAP05-AtRPN10 complex. h Surface diagram of the complex SPL5-SAP05-RPN10 by the superposition of SAP05 from the single complex SPL-SAP05 and SAP05-RPN10. The contact surfaces of SPL-SAP05 and SAP05-RPN10 are referred to as Lobe1 and Lobe2, respectively.

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