{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/101260"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/101260","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Mutations of the glucose-pts in sublancin-resistant B. subtilis 168 ΔSPΒ","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Gancayco, Marc Ryan"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["van der Donk, Wilfred A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-09-04T20:46:49Z","date_published":"2018-09-04T20:46:49Z","updated_at":"2026-07-22T22:24:38Z","subjects":["glycocin","sublancin","mode of action","s-glycosylation"],"languages":["en"],"rights":["Copyright 2018 Marc Gancayco"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/101260","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["van der Donk, Wilfred A."]},{"key":"dc:creator","label":"Author","values":["Gancayco, Marc Ryan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2018-09-04T20:46:49Z","2020-09-05T09:15:29Z","2018-02-27","2018-05"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["glycocin","sublancin","mode of action","s-glycosylation"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2018 Marc Gancayco"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/101260"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2020-05-01","The student, Marc Gancayco, accepted the attached license on 2018-02-27 at 14:30.","The student, Marc Gancayco, submitted this Thesis for approval on 2018-02-27 at 14:38.","This Thesis was approved for publication on 2018-02-27 at 15:11.","DSpace SAF Submission Ingestion Package generated from Vireo submission #12050 on 2018-08-31 at 17:25:14","Made available in DSpace on 2018-09-04T20:46:49Z (GMT). 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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.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2020-05-01","The student, Marc Gancayco, accepted the attached license on 2018-02-27 at 14:30.","The student, Marc Gancayco, submitted this Thesis for approval on 2018-02-27 at 14:38.","This Thesis was approved for publication on 2018-02-27 at 15:11.","DSpace SAF Submission Ingestion Package generated from Vireo submission #12050 on 2018-08-31 at 17:25:14","Made available in DSpace on 2018-09-04T20:46:49Z (GMT). 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