Amino Acid Sequence Studies on the Beta Subunit of Bacterial Luciferase

Peptides comprising 80% of the amino acid sequence of the (beta) subunit of bacterial luciferase from Vibrio harveyi were isolated and their amino acid sequences were determined by Edman degradation. The protein was fragmented by digestion with S. aureus V8 protease, trypsin, trypsin after citraconylation, and by treatment with cyanogen bromide. A substantial proportion of each peptide mixture precipitated and was not amenable to separation. Peptides were isolated by gel filbration, ion exchange chromatography, paper electrophoresis, and high performance reverse phase liquid chromatography. We have found no significant similarity between the (alpha) and (beta) subunits beyond their N-termini. We suggest that the N-terminal similarity may have some role in the function of the protein. Moreover, the (beta) subunit displays no sequence similarity to other flavoproteins, including regions and residues implicated in flavin binding by these enzymes. Therefore, our data do not suggest a role for the (beta) subunit in binding reduced flavin mononucleotide, but they do support the view that luciferase is significantly different from all other flavin monoxygenases.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Thompson, Richard Blair

• Chemistry, Biochemistry

Identifier

(UMI)AAI8203615

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70502