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| THE PRO REGION OF BPTI FACILITATES FOLDING |
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| Author(s): WEISSMAN JS, KIM PS |
| Source: CELL Volume: 71 Issue: 5 Pages: 841-851 Published: NOV 27 1992 |
| Times Cited: 113 References: 57 |
| Abstract: The in vitro folding pathway of bovine pancreatic trypsin inhibitor (BPTI) has been described previously in terms of the disulfide-bonded intermediates that accumulate during folding of the protein. Folding is slow, occurring in hours at pH 7.3, 25-degrees-C. In addition, approximately half of the BPTI molecules become trapped as a dead-end, native-like intermediate. In vivo, BPTI is synthesized as a precursor protein that includes a 13 residue amino-terminal pro region. This pro region contains a cysteine residue. We find that, in vitro, both the rate of formation and the yield of properly folded BPTI are increased substantially in a recombinant model of pro-BPTI. The cysteine residue is necessary for this effect. Moreover, a single cysteine residue, tethered to the carboxy-terminal end of BPTI with a flexible linker of repeating Ser-Gly-Gly residues, is sufficient to assist in disulfide formation. Thus, the pro region appears to facilitate folding by providing a tethered, solvent-accessible, intramolecular thiol-disulfide reagent. |
| Document Type: Article |
| Language: English |
| Reprint Address: WEISSMAN, JS (reprint author), MIT, HOWARD HUGHES MED INST, CAMBRIDGE, MA 02142 USA |
Addresses:
1. MIT, WHITEHEAD INST BIOMED RES, CAMBRIDGE, MA 02142 USA
2. MIT, DEPT PHYS, CAMBRIDGE, MA 02142 USA
3. MIT, DEPT BIOL, CAMBRIDGE, MA 02142 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: JZ633 |
| ISSN: 0092-8674 |
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