A Study of Subunit Folding and Dimer Assembly In Vivo

  • Thomas O. Baldwin
Part of the Industry-University Cooperative Chemistry Program Symposia book series (IUCC)


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.


Folding Process Bacterial Luciferase Luciferase Enzyme Prolyl Residue Proteolytic Inactivation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 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
  2. 2.
    T. W. Cline and J. W. Hastings, Mutationally altered bacterial luciferase. Implications for subunit functions, Biochemistry 11: 3359–3370 (1972).PubMedCrossRefGoogle Scholar
  3. 3.
    J. J. Waddle, T. C. Johnston and T. O. Baldwin, Polypeptide folding and dimerization in bacterial luciferase occur by a concerted mechanism in vivo. Biochemistry 26: 4917–4921 (1987).PubMedCrossRefGoogle Scholar
  4. 4.
    J. Sugihara and T. O. Baldwin, Effects of 3′ end deletions from the Vibrio harveyi luxB gene on luciferase subunit folding and enzyme assembly: Generation of temperature-sensitive polypeptide folding mutants, Biochemistry 27: 2872–2880 (1988).PubMedCrossRefGoogle Scholar
  5. 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. 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
  7. 7.
    L. H. Chen and T. O. Baldwin, Random and site-directed mutagenesis of bacterial luciferase: Investigation of the aldehyde binding site, Biochemistry 28: 2684–2689 (1989).PubMedCrossRefGoogle Scholar
  8. 8.
    A. Gunsalus-Miguel, E. A. Meighen, M. Ziegler-Nicoli, K. H. Nealson and J. W. Hastings, Purification and properties of bacterial luciferases, J. Biol. Chem. 247: 398–404 (1972).PubMedGoogle Scholar
  9. 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
  10. 10.
    J. W. Hastings and G. Weber, Total quantum flux of isotropic sources, J. Opt. Soc. Amer. 53: 1410–1415 (1963).CrossRefGoogle Scholar
  11. 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
  12. 12.
    T. O. Baldwin, J. W. Hastings and P. L. Riley, Proteolytic inactivation of the luciferase from the luminous marine bacterium Beneckea harveyi, J. Biol. Chem. 253: 5551–5554 (1978).PubMedGoogle Scholar
  13. 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
  14. 14.
    D. Njus, T. O. Baldwin and J. W. Hastings, A sensitive assay for proteolytic enzymes using bacterial luciferase as a substrate, Anal. Biochem. 61: 280–287 (1974).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Thomas O. Baldwin
    • 1
  1. 1.The Departments of Biochemistry and Biophysics and of ChemistryTexas A&M UniversityCollege StationUSA

Personalised recommendations