Intramolecular chaperone: the role of the pro-peptide in protein folding.

摘要: Subtilisin, an alkaline serine protease, is produced in the bacterium as pre-pro-subtilisin; pre-peptide of 29 amino acid residues signal peptide essential for secretion prosubtilisin from cytoplasm into culture medium. On other hand, pro-peptide 77 covalently linked to terminal end subtilisin intramolecularly guides folding active enzyme. Importantly, not required enzymatic activity and removed by autoprocessing upon completion protein folding. In this review, I will first summarize all data concerning functions pro-peptide. basis these results, shall discuss a new general concept, intramolecular chaperone explain role