Z.-S. Chong

Deciphering the role of the OmpC-Mla system in bile salt resistance

This study identifies a novel role for the OmpC-Mla system in bile salt resistance in E. coli, independent of its known function in maintaining outer membrane lipid asymmetry.

Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

This study identifies phospholipid binding as a mechanism for DolP localization, revealing its structure and function in Gram-negative bacteria.

Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48 metalloprotease BepA

The paper presents the crystal structure of E. coli BepA, an M48 metalloprotease, and shows that its active site plug regulates function and is conserved across the family.

Structure-function analysis of the Escherichia coli β-barrel assembly enhancing protease BepA suggests a role for a self-inhibitory state

This study presents the crystal structure of BepA, a protease involved in LptD folding, and shows its auto-regulation and role in maintaining outer membrane lipid asymmetry.

Structure of the tripartite motif of KAP1/TRIM28 identifies molecular interfaces required for transcriptional silencing of retrotransposons

This study identifies molecular interfaces in KAP1's RBCC motif critical for self-association and KRAB binding, essential for retrotransposon silencing.

Molecular basis for the maintenance of lipid asymmetry in the outer membrane of Escherichia coli

The paper defines the molecular architecture of the OmpC-MlaA complex in E. coli and shows how it transports phospholipids across the outer membrane to maintain lipid asymmetry.

MCE domain proteins: conserved inner membrane lipid-binding proteins required for outer membrane homeostasis

The paper identifies and characterizes MCE domain proteins in E. coli, showing they localize to the inner membrane and play distinct roles in maintaining outer membrane lipid asymmetry.