A Study of Subunit Folding and Dimer Assembly In Vivo
Bacterial luciferase is a heterodimer, consisting of two nonidentical but homologous subunits, α and β (1). The enzyme has a single active center, that has been shown to be confined primarily, if not exclusively, to the α subunit (1, 2). The role of the β subunit is not known, but there is much support for the assertion that the β subunit is required for activity. The subunits apparently associate with high affinity; there have been no reports demonstrating dissociation of the complex of the wild-type luciferase under non-denaturing conditions.
KeywordsFolding Process Bacterial Luciferase Luciferase Enzyme Prolyl Residue Proteolytic Inactivation
Unable to display preview. Download preview PDF.
- 1.M. M. Ziegler and T. O. Baldwin, Biochemistry of bacterial bioluminescence, in: “Current Topics in Bioenergetics,” Vol. 12, pp. 65–113, Academic Press, New York (1981).Google Scholar
- 5.T. O. Baldwin, T. Berends, T. A. Bunch, T. F. Holzman, S. K. Rausch, L. Shamansky, M. L. Treat and M. M. Ziegler, The cloning of the luciferase structural genes from Vibrio harveyi and the expression of bioluminescence in Escherichia coli. Biochemistry 23: 3663–3667 (1984).PubMedCrossRefGoogle Scholar
- 6.K. Wei, Site specific mutagenesis study of the protein folding process of luciferase, M. S. thesis submitted to the Office of Graduate Studies, Texas A&M University, College Station, Texas (1990).Google Scholar
- 9.J. W. Hastings, T. O. Baldwin and M. Ziegler-Nicoli, Bacterial luciferase: Assay, purification, and properties. in: “Methods in Enzymology,” Vol. 57, pp. 135–152, M. Deluca, ed., Academic Press, New York (1978).Google Scholar
- 11.D. B. Wetlaufer, Folding of protein fragments, in: “Advances in protein chemsitry”, Vol. 34, pp. 61–92, Academic Press, New York (1981).Google Scholar
- 13.T. F. Holzman, P. L. Riley and T. O. Baldwin, Inactivation of luciferase from the luminous marine bacterium Beneckea harveyi by proteases: Evidence for a protease labile region and properties of the protein following inactivation, Arch. Biochem. Biophys. 205: 554–563 (1980).PubMedCrossRefGoogle Scholar