Nichtl, Alfons and Buchner, Johannes and Jaenicke, Rainer and Rudolph, Rainer and Scheibel, Thomas (1998) Folding and association of beta-galactosidase. JOURNAL OF MOLECULAR BIOLOGY, 282 (5). pp. 1083-1091. ISSN 0022-2836, 1089-8638
Full text not available from this repository. (Request a copy)Abstract
beta-D-Galactosidase from Escherichia coli is one of the largest tetrameric enzymes known at present. Although its physiological importance, the regulation of its synthesis, its enzymatic properties and its structure are well established, little is known about the stability and the folding pathway of this enzyme. Here we show that the overall folding mechanism of chemically denatured beta-galactosidase consists of three stages: (i) formation of elements of secondary structure; (ii) collapse to subdomains and structured monomers; (iii) association to the native quaternary structure via dimeric intermediates. The first rate-limiting step is the association of structured monomers to form dimers in a bi-molecular reaction, with a rate constant of 4.3 x 10(3) M-1 s(-1) at 20 degrees C. The second rate-limiting uni-molecular folding step leads to dimers which are competent for further association, with a rate constant of 0.5 x 10(-3) s(-1) at 20 degrees C. Tetramers form from these dimers in a fast reaction. By determining a similar mechanism for alpha-complementation of beta-galactosidase fragments it could be confirmed that beta-galactosidase follows a consecutive bi-uni-molecular mechanism of folding and association. (C) 1998 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MOLECULAR CHAPERONE MACHINES; MUSCLE LACTIC-DEHYDROGENASE; ESCHERICHIA-COLI; 3-DIMENSIONAL STRUCTURE; ALPHA-COMPLEMENTATION; IN-VITRO; PROTEIN; RECONSTITUTION; AGGREGATION; KINETICS; alpha-complementation; protein stability; chaperones |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Feb 2023 07:18 |
| Last Modified: | 23 Feb 2023 07:18 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49440 |
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