Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation.

ABSTRACT: In eukaryotes, targeted protein degradation (TPD) typically depends on a series of interactions among ubiquitin ligases that transfer ubiquitin molecules to substrates leading to degradation by the 26S proteasome. We previously identified that the bacterial effector protein SAP05 mediates ubiquitin-independent TPD. SAP05 forms a ternary complex via interactions with the von Willebrand Factor Type A (vWA) domain of the proteasomal ubiquitin receptor Rpn10 and the zinc-finger (ZnF) domains of the SQUAMOSA-PROMOTER BINDING PROTEIN-LIKE (SPL) and GATA BINDING FACTOR (GATA) transcription factors (TFs). This leads to direct TPD of the TFs by the 26S proteasome. Here, we report the crystal structures of the SAP05-Rpn10^vWA complex at 2.17 Å resolution and of the SAP05-SPL5^ZnF

SUBMITTER: Liu Q 

PROVIDER: S-EPMC10710061 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature