Study on Caseinolytic Protease Chaperones and its Cognate Adaptors of Leptospira Interrogans

Abstract

Bacterial Caseinolytic protease (Clp) systems are central to protein quality control, mediating the ATP-dependent degradation of misfolded or aggregated proteins. In Leptospira interrogans, the Clp machinery comprises two proteolytic isoforms (ClpP1 and ClpP2), multiple ATPase chaperones (ClpA, ClpC, ClpX), and adaptor proteins (ClpS1, ClpS2). The core protease forms a hetero-tetradecameric ClpP1P2 complex that exhibits intrinsic peptidase activity toward short peptides, while degradation of protein substrates requires association with ATPase chaperones such as ClpX. However, the structural basis for selective activation and regulation of leptospiral Clp components remains poorly understood.