Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis - PubMed (original) (raw)
Comparative Study
Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis
M Hahn et al. Proc Natl Acad Sci U S A. 1994.
Abstract
A jellyroll beta-sandwich protein, the Bacillus beta-glucanase H(A16-M), is used to probe the role of N-terminal peptide regions in protein folding in vivo. A gene encoding H(A16-M) is rearranged to place residues 1-58 of the protein behind a signal peptide and residues 59-214. The rearranged gene is expressed in Escherichia coli. The resultant circularly permuted protein, cpA16M-59, is secreted into the periplasm, correctly processed, and folded into a stable and active enzyme. Crystal structure analysis at 2.0-A resolution, R = 15.3%, shows cpA16M-59 to have a three-dimensional structure nearly identical with that of the parent beta-glucanase. An analogous experiment based on the wild-type Bacillus macerans beta-glucanase, giving rise to the circularly permuted variant cpMAC-57, yields the same results. Folding of these proteins, therefore, is not a vectorial process depending on the conformation adopted by their native N-terminal oligopeptides after ribosomal synthesis and translocation through the cytoplasmic membrane.
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References
- J Bacteriol. 1990 Jul;172(7):3837-41 - PubMed
- Methods Enzymol. 1985;115:157-71 - PubMed
- J Mol Biol. 1983 Apr 5;165(2):407-13 - PubMed
- Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11980-4 - PubMed
- Mol Gen Genet. 1990 Jul;222(2-3):278-83 - PubMed
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