Mutations of the glucose-pts in sublancin-resistant B. subtilis 168 ΔSPΒ
Gancayco, Marc Ryan
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https://hdl.handle.net/2142/101260
Description
Title
Mutations of the glucose-pts in sublancin-resistant B. subtilis 168 ΔSPΒ
Author(s)
Gancayco, Marc Ryan
Issue Date
2018-02-27
Director of Research (if dissertation) or Advisor (if thesis)
van der Donk, Wilfred A.
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
M.S.
Degree Level
Thesis
Keyword(s)
glycocin
sublancin
mode of action
s-glycosylation
Abstract
The mode of action of the glycocins is still unknown. The glycocin family is unusual due to the rarity of glycosylated peptides in bacteria and of cysteine S-glycosylations in general. S-glycosylation of cysteine has previously been shown to result in a metabolically more stable conjugation than the more common O-glycosylation of serine. This stabilization is supported by the high stability of sublancin and may explain the need for glycosylation in sublancin for antimicrobial activity. Previous studies have shown that the deletion of and mutations in the glucose phosphotransferase system confer resistance to sublancin. In this work we add to this knowledge by generating new sublancin-resistant mutants in B. subtilis 168 ΔSPβ. The mutations found support previous findings but also demonstrate the need to look for larger genome changes that may affect the regulation of the glucose phosphotransferase system.
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