{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/19536"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/19536","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation","abstract":"U of I Only","abstract_html":"U of I Only","abstract_has_math":false,"creators":["Henry, Michael Francis"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Cronan, John E."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:10:35Z","date_published":"2011-05-07T12:10:35Z","updated_at":"2026-07-22T22:25:14Z","subjects":["Biology, Molecular","Biology, Microbiology"],"languages":["eng"],"rights":["Copyright 1992 Henry, Michael Francis"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9236482","(UMI)AAI9236482"],"render_values":[{"text":"AAI9236482","href":null,"code":true},{"text":"(UMI)AAI9236482","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/19536","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cronan, John E."]},{"key":"dc:creator","label":"Author","values":["Henry, Michael Francis"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:10:35Z","10000-01-01","1992"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"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":["Biology, Molecular","Biology, Microbiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1992 Henry, Michael Francis"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9236482","(UMI)AAI9236482","http://hdl.handle.net/2142/19536"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["U of I Only","I have examined fadR regulation of fabA expression using a variety of biochemical and genetic techniques. First, I showed that introduction of fadR null alleles into strains carrying any of several different fabA temperature-sensitive alleles lowered the permissive growth temperature of the strain. The increased temperature sensitivity was shown to result from a decrease in the amount of unsaturated fatty acids (UFAs) present in the membranes of these strains. Dehydrase (FabA) activity was then assayed in isogenic $fad\\sp+$ and fadR null strains and found to be decreased 10 to 12-fold in the fadR null strains. These results, in combination with results obtained by fabA-reporter-gene fusions (lacZ and cat) and direct Northern analysis, indicated transcriptional activation. Northern analysis also showed that the fabA gene was transcribed from two promoters located just upstream from the coding sequence; one of which was activated in a $fadR\\sp+$ strain.","FadR DNA-binding to upstream elements of fabA was shown by mobility shift assays using both crude cell extracts, and radiochemically pure FadR protein synthesized in vitro. Additional DNA-binding assays defined the DNA-binding region to a 17-bp consensus sequence. Similar sequences were identified upstream of the fadL and the fadAB genes; both transcriptionally repressed by FadR. Finally, a combination of in vivo and in vitro assays were used to demonstrate that FadR DNA-binding was inhibited in the presence of long-chain acyl-CoAs.","This study was facilitated by developing a technique which uses the cointegrate intermediate of transposon Tn1000 as a means to lower the copy number of ColE1-type plasmids. Using in vitro techniques, the DNA sequence of the Tn1000 transposon was altered so that cointegrate formation occurs but resolution by the site-specific recombination pathway is blocked. When this transposon was resident on an F factor-derived plasmid, a cointegrate was formed between a multicopy ColE1-type plasmid and the conjugative F plasmid. Conjugational transfer of this cointegrate into a polA strain resulted in a stable cointegrate in which replication from the ColE1 plasmid was inhibited and replication proceeded only from the single-copy F factor replication origin. (Abstract shortened with permission of author.)","Made available in DSpace on 2011-05-07T12:10:35Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9236482.pdf: 5021639 bytes, checksum: 5fdc83d62a1e8f92b7ecc11eb3b73e64 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:37:42Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:15:33-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission"]},{"key":"dc:title","label":"Title","values":["Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation"]}]}],"canonical_facts":{"dc:contributor":["Cronan, John E."],"dc:creator":["Henry, Michael Francis"],"dc:date":["2011-05-07T12:10:35Z","10000-01-01","1992"],"dc:description":["U of I Only","I have examined fadR regulation of fabA expression using a variety of biochemical and genetic techniques. First, I showed that introduction of fadR null alleles into strains carrying any of several different fabA temperature-sensitive alleles lowered the permissive growth temperature of the strain. The increased temperature sensitivity was shown to result from a decrease in the amount of unsaturated fatty acids (UFAs) present in the membranes of these strains. Dehydrase (FabA) activity was then assayed in isogenic $fad\\sp+$ and fadR null strains and found to be decreased 10 to 12-fold in the fadR null strains. These results, in combination with results obtained by fabA-reporter-gene fusions (lacZ and cat) and direct Northern analysis, indicated transcriptional activation. Northern analysis also showed that the fabA gene was transcribed from two promoters located just upstream from the coding sequence; one of which was activated in a $fadR\\sp+$ strain.","FadR DNA-binding to upstream elements of fabA was shown by mobility shift assays using both crude cell extracts, and radiochemically pure FadR protein synthesized in vitro. Additional DNA-binding assays defined the DNA-binding region to a 17-bp consensus sequence. Similar sequences were identified upstream of the fadL and the fadAB genes; both transcriptionally repressed by FadR. Finally, a combination of in vivo and in vitro assays were used to demonstrate that FadR DNA-binding was inhibited in the presence of long-chain acyl-CoAs.","This study was facilitated by developing a technique which uses the cointegrate intermediate of transposon Tn1000 as a means to lower the copy number of ColE1-type plasmids. Using in vitro techniques, the DNA sequence of the Tn1000 transposon was altered so that cointegrate formation occurs but resolution by the site-specific recombination pathway is blocked. When this transposon was resident on an F factor-derived plasmid, a cointegrate was formed between a multicopy ColE1-type plasmid and the conjugative F plasmid. Conjugational transfer of this cointegrate into a polA strain resulted in a stable cointegrate in which replication from the ColE1 plasmid was inhibited and replication proceeded only from the single-copy F factor replication origin. (Abstract shortened with permission of author.)","Made available in DSpace on 2011-05-07T12:10:35Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9236482.pdf: 5021639 bytes, checksum: 5fdc83d62a1e8f92b7ecc11eb3b73e64 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:37:42Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:15:33-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission"],"dc:identifier":["AAI9236482","(UMI)AAI9236482","http://hdl.handle.net/2142/19536"],"dc:language":["eng"],"dc:rights":["Copyright 1992 Henry, Michael Francis"],"dc:subject":["Biology, Molecular","Biology, Microbiology"],"dc:title":["Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:14Z"}