Biophysical and NMR analysis reveals binding affinity between HAX1 and CLPB proteins.

ABSTRACT: HCLS1-associated protein X-1 (HAX1) is a multifunctional mitochondrial protein involved in the regulation of apoptosis, a crucial process of programmed cell death, and mRNA processing. Despite its significance, limited structural data is available for HAX1, hindering a comprehensive understanding of its biological function. Notably, the caseinolytic mitochondrial matrix peptidase chaperone subunit B (CLPB) has been identified as an interacting partner of HAX1, yet the biophysical properties and binding affinity governing their interaction remain poorly defined. In this study, we present a thorough biophysical characterization of full-length human HAX1 and CLPB, accomplished through recombinant expression and purification. By employing size exclusion chromatography, dynamic light scattering

SUBMITTER: Zhang H 

PROVIDER: S-EPMC12406527 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature