A Transient π-π or Cation-π Interaction between Degron and Degrader Dual Residues: A Key Step for the Substrate Recognition and Discrimination in the Processive Degradation of SulA by ClpYQ (HslUV) Protease in Escherichia coli.

ABSTRACT: The Escherichia coli ATP-dependent ClpYQ protease constitutes ClpY ATPase/unfoldase and ClpQ peptidase. The Tyr^91st residue within the central pore-I site of ClpY-hexamer is important for unfolding and translocating substrates into the catalytic site of ClpQ. We have identified the degron site (GFIMRP^147th) of SulA, a cell-division inhibitor recognized by ClpYQ and that the Phe^143rd residue in degron site is necessary for SulA native folded structure. However, the functional association of this degron site with the ClpYQ degrader is unknown. Here, we investigated the molecular insights into substrate recognition and discrimination by the ClpYQ protease. We found that the point mutants ClpY^Y91FQ, ClpY^Y91HQ, and ClpY^Y91W

SUBMITTER: Lin CH 

PROVIDER: S-EPMC10743992 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature