{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70536"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70536","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Degradation of Aspartate Transcarbamylase in Growing and Starved Bacillus Subtilis Cells","abstract":"Aspartate transcarbamylase (ATCase) is degraded upon starvation of Bacillus subtilis cells for carbon or nitrogen. The rate of ATCase degradation in exponentially growing B. subtilis cells was determined by measurement of enzyme activity after the addition of uridine to repress further enzyme synthesis and by specific immunoprecipitation of the enzyme from cells grown in the presence of (('3)H)leucine. ATCase was degraded with a half-life of about 1.5h in cells growing on a glucose-salts minimal medium with NH(,4)('+) ions as the sole source of nitrogen. Replacement of NH(,4)('+) in this medium with a combination of the amino acids aspartate, glutamate, isoleucine, proline, and threonine reduced the degradation rate to an undetectable level. Various other amino acids had smaller effects on the rate of degradation. The carbon source also influenced the degradation rate, but to a smaller extent than the nitrogen source. The effects of these nutritional variables on the rate of bulk protein turnover in growing cells were generally similar to their effects on degradation of ATCase.","abstract_html":"Aspartate transcarbamylase (ATCase) is degraded upon starvation of Bacillus subtilis cells for carbon or nitrogen. The rate of ATCase degradation in exponentially growing B. subtilis cells was determined by measurement of enzyme activity after the addition of uridine to repress further enzyme synthesis and by specific immunoprecipitation of the enzyme from cells grown in the presence of (('3)H)leucine. ATCase was degraded with a half-life of about 1.5h in cells growing on a glucose-salts minimal medium with NH(,4)('+) ions as the sole source of nitrogen. Replacement of NH(,4)('+) in this medium with a combination of the amino acids aspartate, glutamate, isoleucine, proline, and threonine reduced the degradation rate to an undetectable level. Various other amino acids had smaller effects on the rate of degradation. The carbon source also influenced the degradation rate, but to a smaller extent than the nitrogen source. The effects of these nutritional variables on the rate of bulk protein turnover in growing cells were generally similar to their effects on degradation of ATCase.","abstract_has_math":false,"creators":["Bond, Richard William"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-15T23:43:48Z","date_published":"2014-12-15T23:43:48Z","updated_at":"2026-07-22T22:26:03Z","subjects":["Chemistry, Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8502074"],"render_values":[{"text":"(UMI)AAI8502074","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70536","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Bond, Richard William"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:43:48Z","10000-01-01","1984"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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":["Chemistry, Biochemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70536","(UMI)AAI8502074"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Aspartate transcarbamylase (ATCase) is degraded upon starvation of Bacillus subtilis cells for carbon or nitrogen. The rate of ATCase degradation in exponentially growing B. subtilis cells was determined by measurement of enzyme activity after the addition of uridine to repress further enzyme synthesis and by specific immunoprecipitation of the enzyme from cells grown in the presence of (('3)H)leucine. ATCase was degraded with a half-life of about 1.5h in cells growing on a glucose-salts minimal medium with NH(,4)('+) ions as the sole source of nitrogen. Replacement of NH(,4)('+) in this medium with a combination of the amino acids aspartate, glutamate, isoleucine, proline, and threonine reduced the degradation rate to an undetectable level. Various other amino acids had smaller effects on the rate of degradation. The carbon source also influenced the degradation rate, but to a smaller extent than the nitrogen source. The effects of these nutritional variables on the rate of bulk protein turnover in growing cells were generally similar to their effects on degradation of ATCase.","Addition of protein synthesis inhibitors to B. subtilis cells grown in minimal medium under conditions in which ATCase was either stable or unstable blocked the rapid degradation of ATCase. This is in contrast with results from cells grown in a supplemented nutrient broth medium. Degradation of ATCase was also deficient in growing and starved relA and relC mutants, but these effects were not correlated with differences in the intracellular level of guanosine polyphosphates.","An assay for ATCase-degrading activity in vitro was developed to test the involvement of ribosomally associated factors in ATCase degradation. Cells were fractionated, and activity was found in both the crude membrane and ribosomal fractions but not in the soluble fraction. The activity in vitro was not correlated with ATCase degradation in vivo. Activity was present in fractions from cells in which ATCase was stable. Also, ATCase degradation in vitro was not affected by mutations in the relA or relC proteins.","Made available in DSpace on 2014-12-15T23:43:48Z (GMT). No. of bitstreams: 1 8502074.pdf: 5492354 bytes, checksum: 2d0dd07c7c6e16a852ce4c90fe0cf4d4 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70702 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","156 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."]},{"key":"dc:title","label":"Title","values":["Degradation of Aspartate Transcarbamylase in Growing and Starved Bacillus Subtilis Cells"]}]}],"canonical_facts":{"dc:creator":["Bond, Richard William"],"dc:date":["2014-12-15T23:43:48Z","10000-01-01","1984"],"dc:description":["Aspartate transcarbamylase (ATCase) is degraded upon starvation of Bacillus subtilis cells for carbon or nitrogen. The rate of ATCase degradation in exponentially growing B. subtilis cells was determined by measurement of enzyme activity after the addition of uridine to repress further enzyme synthesis and by specific immunoprecipitation of the enzyme from cells grown in the presence of (('3)H)leucine. ATCase was degraded with a half-life of about 1.5h in cells growing on a glucose-salts minimal medium with NH(,4)('+) ions as the sole source of nitrogen. Replacement of NH(,4)('+) in this medium with a combination of the amino acids aspartate, glutamate, isoleucine, proline, and threonine reduced the degradation rate to an undetectable level. Various other amino acids had smaller effects on the rate of degradation. The carbon source also influenced the degradation rate, but to a smaller extent than the nitrogen source. The effects of these nutritional variables on the rate of bulk protein turnover in growing cells were generally similar to their effects on degradation of ATCase.","Addition of protein synthesis inhibitors to B. subtilis cells grown in minimal medium under conditions in which ATCase was either stable or unstable blocked the rapid degradation of ATCase. This is in contrast with results from cells grown in a supplemented nutrient broth medium. Degradation of ATCase was also deficient in growing and starved relA and relC mutants, but these effects were not correlated with differences in the intracellular level of guanosine polyphosphates.","An assay for ATCase-degrading activity in vitro was developed to test the involvement of ribosomally associated factors in ATCase degradation. Cells were fractionated, and activity was found in both the crude membrane and ribosomal fractions but not in the soluble fraction. The activity in vitro was not correlated with ATCase degradation in vivo. Activity was present in fractions from cells in which ATCase was stable. Also, ATCase degradation in vitro was not affected by mutations in the relA or relC proteins.","Made available in DSpace on 2014-12-15T23:43:48Z (GMT). No. of bitstreams: 1 8502074.pdf: 5492354 bytes, checksum: 2d0dd07c7c6e16a852ce4c90fe0cf4d4 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70702 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","156 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."],"dc:identifier":["http://hdl.handle.net/2142/70536","(UMI)AAI8502074"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Degradation of Aspartate Transcarbamylase in Growing and Starved Bacillus Subtilis Cells"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:03Z"}