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Folding and association of β-galactosidase

Title data

Nichtl, Alfons ; Buchner, Johannes ; Jaenicke, Rainer ; Rudolph, Rainer ; Scheibel, Thomas:
Folding and association of β-galactosidase.
In: Journal of Molecular Biology. Vol. 282 (1998) Issue 5 . - pp. 1083-1091.
ISSN 0022-2836

Abstract in another language

β-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 β-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 4.3×103 M−1 s−1at 20°C. The second rate-limiting uni-molecular folding step leads to dimers which are competent for further association, with a rate constant of 0.5×10−3 s−1at 20°C. Tetramers form from these dimers in a fast reaction. By determining a similar mechanism for α-complementation of β-galactosidase fragments it could be confirmed that β-galactosidase follows a consecutive bi-uni-molecular mechanism of folding and association.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: α-complementation; protein stability; chaperones
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: No
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 01 Oct 2015 12:45
Last Modified: 08 Jul 2022 13:30