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Dimerization by Domain Hybridization Bestows Chaperone and Isomerase Activities.
- Source :
-
Journal of Biological Chemistry . 10/31/2003, Vol. 278 Issue 44, p43292-43298. 7p. 1 Black and White Photograph, 3 Diagrams, 3 Charts, 4 Graphs. - Publication Year :
- 2003
-
Abstract
- Thioredoxin, DsbA, the N-terminal active-site domain a and the non-active-site domain b of protein-disulfide isomerase are all monomeric with a thioredoxin fold, and each exhibits Iow or no isomerase and chaperone activity. We have linked the N terminus of the above four monomers, individually, to the C terminus of the N-terminal domain of DsbC via the flexible linker helix of the latter to produce four domain hybrids, DsbCnTrx, DsbCn-DsbA, DsbCn-PDIa, and DsbCn-PDIb. These four hybrid proteins form homodimers, and except for DsbCn-PDIb they exhibit new or greatly elevated isomerase as well as chaperone activity. Three-dimensional structure prediction indicates that all the four domain hybrids adopt DsbC-like V-shaped structure with a broad uncharged cleft between the two arms for binding of non-native protein folding intermediates. The results provide strong evidence that dimerization creates chaperone and isomerase activity for monomeric thiol-protein oxidases or reductases, and suggesting a pathway for proteins to acquire new functions and/or higher biological efficiency during evolution. [ABSTRACT FROM AUTHOR]
- Subjects :
- *THIOREDOXIN
*PROTEINS
*THIOLS
Subjects
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 278
- Issue :
- 44
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 11562506
- Full Text :
- https://doi.org/10.1074/jbc.M306945200