Usage of Cell-Free Protein Synthesis in Post-Translational Modification of μ-Conopeptide PIIIA.

ABSTRACT: The post-translational modifications of conopeptides are the most complicated modifications to date and are well-known and closely related to the activity of conopeptides. The hydroxylation of proline in conopeptides affects folding, structure, and biological activity, and prolyl 4 hydroxylase has been characterized in Conus literatus. However, the hydroxylation machinery of proline in conopeptides is still unclear. In order to address the hydroxylation mechanism of proline in μ-PIIIA, three recombinant plasmids encoding different hybrid precursors of μ-PIIIA were constructed and crossly combined with protein disulfide isomerase, prolyl 4 hydroxylase, and glutaminyl cyclase in a continuous exchange cell-free protein system. The findings showed that prolyl 4 hydroxylase might recogni

SUBMITTER: Liu Y 

PROVIDER: S-EPMC10455749 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature