{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84787"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84787","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Chemotactic Sensory Transduction in Bacillus Subtilis: A New Enzyme and a New Pathway","abstract":"Chemotaxis towards substrates of the phosphoenolpyruvate-dependent-phosphotransferase system (PTS) in E. coli is accomplished using a chemoreceptor-independent signaling circuit in which phosphoryl flux through the PTS is monitored and used directly to modulate the activity of the chemotactic kinase. In contrast, chemotaxis towards PTS carbohydrates by B. subtilis requires the transmembrane chemoreceptor McpC; therefore, B. subtilis must employ a different sensory circuit to mediate such chemotaxis. The results in this study indicate that the sensory circuit mediating chemotaxis towards PTS carbohydrates utilizes the cytoplasmic methyl-accepting subdomain of McpC as a sensor for PTS stimuli. This receptor subdomain has not been reported to function as a sensor of chemical stimuli for any known chemoreceptor.","abstract_html":"Chemotaxis towards substrates of the phosphoenolpyruvate-dependent-phosphotransferase system (PTS) in E. coli is accomplished using a chemoreceptor-independent signaling circuit in which phosphoryl flux through the PTS is monitored and used directly to modulate the activity of the chemotactic kinase. In contrast, chemotaxis towards PTS carbohydrates by B. subtilis requires the transmembrane chemoreceptor McpC; therefore, B. subtilis must employ a different sensory circuit to mediate such chemotaxis. The results in this study indicate that the sensory circuit mediating chemotaxis towards PTS carbohydrates utilizes the cytoplasmic methyl-accepting subdomain of McpC as a sensor for PTS stimuli. This receptor subdomain has not been reported to function as a sensor of chemical stimuli for any known chemoreceptor.","abstract_has_math":false,"creators":["Kristich, Christopher James"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Geroge W. Ordal"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:27:54Z","date_published":"2015-09-25T22:27:54Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3070359"],"render_values":[{"text":"(MiAaPQ)AAI3070359","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84787","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Geroge W. 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In contrast, chemotaxis towards PTS carbohydrates by B. subtilis requires the transmembrane chemoreceptor McpC; therefore, B. subtilis must employ a different sensory circuit to mediate such chemotaxis. The results in this study indicate that the sensory circuit mediating chemotaxis towards PTS carbohydrates utilizes the cytoplasmic methyl-accepting subdomain of McpC as a sensor for PTS stimuli. This receptor subdomain has not been reported to function as a sensor of chemical stimuli for any known chemoreceptor.","Made available in DSpace on 2015-09-25T22:27:54Z (GMT). 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