Discovery and characterization of a set of peptide-modifying heme oxygenase-like domain-containing oxidases
Battiste, Alexander Jason
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Permalink
https://hdl.handle.net/2142/130026
Description
Title
Discovery and characterization of a set of peptide-modifying heme oxygenase-like domain-containing oxidases
Author(s)
Battiste, Alexander Jason
Issue Date
2025-07-17
Director of Research (if dissertation) or Advisor (if thesis)
Mitchell, Douglas A
Doctoral Committee Chair(s)
Mitchell, Douglas A
Committee Member(s)
Metcalf, William W
Hergenrother, Paul J
Zhao, Huimin
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Ribosomally synthesized and post-translationally modified peptides (RiPPs)
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a class of natural products made through the post-translational modification of genetically encoded and ribosomally synthesized precursor peptides. Because of their wide array of bioactivities, it would be desirable to be able to catalog all RiPPs, both in terms of their structure and their bioactivities. However, while bioinformatic methods for RiPP identification have improved dramatically in the past decade, it is still challenging to identify RiPPs from new classes. This is especially true if the new RiPP class does not rely on enzymes that are homologous to enzymes from known classes of RiPPs. Even if a RiPP biosynthetic gene cluster (BGC) can be identified, there are often multiple residues that could possibly be modified by the enzymes, and it is not clear which of them will get modified. To determine the structure, and to determine the bioactivity of the natural product, the product must be purified, which can be a time consuming process. Two methods are described here, one method for the rapid assembly of RiPP BGCs into expression plasmids to facilitate their isolation from heterologous hosts, and one bioinformatic method for the discovery of new classes of RiPPs. Using these methods, a number of RiPPs from known classes are characterized, including some with bioactivities against known pathogens, and a new class of RiPPs is discovered. These new RiPPs are modified by a set of heme oxygenase domain-containing oxygenases (HDOs), an emerging class of metal dependent enzymes.
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