Intramolecular chaperone: the role of the pro-peptide in protein folding.
Subtilisin, an alkaline serine protease, is produced in the bacterium as pre-pro-subtilisin; the pre-peptide of 29 amino acid residues is the signal peptide essential for the secretion of prosubtilisin from the cytoplasm into the culture medium. On the other hand, the pro-peptide of 77 residues covalently linked to the amino terminal end of the subtilisin intramolecularly guides the folding of subtilisin into the active enzyme. Importantly, the pro-peptide is not required for the enzymatic activity and is removed intramolecularly by autoprocessing upon the completion of the protein folding. In this review, I will first summarize all the data concerning the functions of the subtilisin pro-peptide. On the basis of these results, I shall discuss a new general concept, an intramolecular chaperone to explain the essential role of the pro-peptide in protein folding.
Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Rutgers, Piscataway.
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Inouye
D000595:Amino Acid Sequence; D001665:Binding Sites; D018833:Chaperonins; D004792:Enzyme Precursors / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013381:Subtilisins / Q000378:metabolism*
D004792:Enzyme Precursors; D010446:Peptide Fragments; D021382:Protein Sorting Signals; D011506:Proteins; C057107:prosubtilisin; D013381:Subtilisins; C049752:preprosubtilisin; D018833:Chaperonins