Ajitesh Lunge

Ajitesh Lunge1,2, Radhika Gupta3,4, Eira Choudhary1,5 and Nisheeth Agarwal1* 1Translational Health Science and Technology Institute, National Capital Region Biotech Science Cluster, Faridabad, India 2Jawaharlal Nehru University, New Delhi, India 3Daulat Ram College, University of Delhi, Delhi, India 4Institute of Genomics and Integrative Biology, New Delhi, India 5Symbiosis International (Deemed University), Lavale, Pune, India ↵*For correspondence: Nisheeth Agarwal, nisheeth{at}thsti.res.in.

Abstract The human pathogen Mycobacterium tuberculosis (Mtb) harbors a well-orchestrated caseinolytic protease (Clp) proteolytic machinery, consisting of two oligomeric segments, a barrel-shaped heterotetradecameric protease core comprising ClpP1 and ClpP2 subunits, and hexameric ring-like ATP-dependent unfoldases composed of ClpX or ClpC1. The roles of the ClpP1P2 protease subunits are well established in Mtb, but the potential roles of the associated unfoldases, such as ClpC1, remain elusive.