Mutations of the glucose-pts in sublancin-resistant B. subtilis 168 ΔSPΒ

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.

Name thesis:degree_name

M.S.

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2018

Author dc:creator

• Gancayco, Marc Ryan

Contributors dc:contributor

• van der Donk, Wilfred A.

• glycocin
• sublancin
• mode of action
• s-glycosylation

Statement dc:rights

• Copyright 2018 Marc Gancayco

Language dc:language

en

Handle dc:identifier

http://hdl.handle.net/2142/101260

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/101260