{"id":{"repo_id":"uvic","oai_identifier":"oai:dspace.library.uvic.ca:1828/20060"},"canonical_url":"https://search.dev.ndltd.org/etd/uvic/oai:dspace.library.uvic.ca:1828/20060","repository":{"repo_id":"uvic","name":"University of Victoria (Canada)","base_url":"https://dspace.library.uvic.ca/server/oai/request"},"display":{"title":"Isolation and characterization of certain ribosomal domains : the 5S RNA-protein domain from Escherichia coli and the 'A' protein domain from wheat germ","abstract":"Ribosomes are believed to be composed of many structurally and functionally important, protein-protein and RNA-protein domains. Two of these domains have been investigated. These are the 5S RNA-protein domain and the ribosomal 'A' protein domain. (i) An attempt has been made to isolate the 5S RNA-protein domain from the large ribosomal subunit of the eubacterium Escherichia coli, as the first step in a project to isolate this domain from an archaebacterial source. E. coli 50S subunits were subjected to a low concentration of Mg²⁺ (2 mM), EDTA•Na₂(10 mM) and NH₄Cl (1 M), (A. Liljas, unpublished), as a possible method to remove the 5S RNA­ protein complex from the ribosome. The suspension was centrifuged at 35,000 rpm for 15 hours in a Beckman Ti60 rotor and the supernatant obtained was passed through a 5-20% sucrose gradient. A fraction was obtained which contained several r-proteins and 5S RNA. In an attempt to purify the complex. further, the fraction was passed through an S200 column. Although evidence suggests that a complex was obtained, attempts to identify the composition were not successful. (ii) An attempt was also made to isolate the ribosomal 'A' protein domain, (equivalent to EL7/EL12-EL10 from E. coli), from the large subunit of wheat germ ribosomes, and to isolate and characterize its individual components. A putative complex has been found , of molecular weight 58, 000, containing three r-proteins with molecular weights 15, 000, 13, 700 and 32, 000 respectively. The N-terminal portions of each of these r-proteins has been sequenced. One protein (protein 8) was identified by its sequence as the ribosomal 'A' protein , while another (protein 7) has no homology with the N-terminal portion to protein 8. The third protein (protein 10) has been obtained and differs substantially from the other two proteins in molecular weight, but shows an identical N-terminal amino acid sequence to protein 7.","abstract_html":"Ribosomes are believed to be composed of many structurally and functionally important, protein-protein and RNA-protein domains. Two of these domains have been investigated. These are the 5S RNA-protein domain and the ribosomal 'A' protein domain. (i) An attempt has been made to isolate the 5S RNA-protein domain from the large ribosomal subunit of the eubacterium Escherichia coli, as the first step in a project to isolate this domain from an archaebacterial source. E. coli 50S subunits were subjected to a low concentration of Mg²⁺ (2 mM), EDTA•Na₂(10 mM) and NH₄Cl (1 M), (A. Liljas, unpublished), as a possible method to remove the 5S RNA­ protein complex from the ribosome. The suspension was centrifuged at 35,000 rpm for 15 hours in a Beckman Ti60 rotor and the supernatant obtained was passed through a 5-20% sucrose gradient. A fraction was obtained which contained several r-proteins and 5S RNA. In an attempt to purify the complex. further, the fraction was passed through an S200 column. Although evidence suggests that a complex was obtained, attempts to identify the composition were not successful. (ii) An attempt was also made to isolate the ribosomal 'A' protein domain, (equivalent to EL7/EL12-EL10 from E. coli), from the large subunit of wheat germ ribosomes, and to isolate and characterize its individual components. A putative complex has been found , of molecular weight 58, 000, containing three r-proteins with molecular weights 15, 000, 13, 700 and 32, 000 respectively. The N-terminal portions of each of these r-proteins has been sequenced. One protein (protein 8) was identified by its sequence as the ribosomal 'A' protein , while another (protein 7) has no homology with the N-terminal portion to protein 8. The third protein (protein 10) has been obtained and differs substantially from the other two proteins in molecular weight, but shows an identical N-terminal amino acid sequence to protein 7.","abstract_has_math":false,"creators":["Watt, Paul William"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1982,"date_issued":"1982","date_published":"1982","updated_at":"2026-08-21T16:50:31Z","subjects":[],"languages":[],"rights":["Available to the World Wide Web"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/1828/20060","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"source_record":{"url":"https://dspace.library.uvic.ca/server/oai/request?verb=GetRecord&metadataPrefix=dim&identifier=oai%3Adspace.library.uvic.ca%3A1828%2F20060","prefix":"dim"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Watt, Paul William"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2024-08-15T20:13:35Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2024-08-15T20:13:35Z"]},{"key":"dc:date.issued","label":"Date","values":["1982"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["Available to the World Wide Web"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/1828/20060"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Ribosomes are believed to be composed of many structurally and functionally important, protein-protein and RNA-protein domains. Two of these domains have been investigated. These are the 5S RNA-protein domain and the ribosomal 'A' protein domain. (i) An attempt has been made to isolate the 5S RNA-protein domain from the large ribosomal subunit of the eubacterium Escherichia coli, as the first step in a project to isolate this domain from an archaebacterial source. E. coli 50S subunits were subjected to a low concentration of Mg²⁺ (2 mM), EDTA•Na₂(10 mM) and NH₄Cl (1 M), (A. Liljas, unpublished), as a possible method to remove the 5S RNA­ protein complex from the ribosome. The suspension was centrifuged at 35,000 rpm for 15 hours in a Beckman Ti60 rotor and the supernatant obtained was passed through a 5-20% sucrose gradient. A fraction was obtained which contained several r-proteins and 5S RNA. In an attempt to purify the complex. further, the fraction was passed through an S200 column. Although evidence suggests that a complex was obtained, attempts to identify the composition were not successful. (ii) An attempt was also made to isolate the ribosomal 'A' protein domain, (equivalent to EL7/EL12-EL10 from E. coli), from the large subunit of wheat germ ribosomes, and to isolate and characterize its individual components. A putative complex has been found , of molecular weight 58, 000, containing three r-proteins with molecular weights 15, 000, 13, 700 and 32, 000 respectively. The N-terminal portions of each of these r-proteins has been sequenced. One protein (protein 8) was identified by its sequence as the ribosomal 'A' protein , while another (protein 7) has no homology with the N-terminal portion to protein 8. The third protein (protein 10) has been obtained and differs substantially from the other two proteins in molecular weight, but shows an identical N-terminal amino acid sequence to protein 7."]},{"key":"dc:title","label":"Title","values":["Isolation and characterization of certain ribosomal domains : the 5S RNA-protein domain from Escherichia coli and the 'A' protein domain from wheat germ"]}]}],"canonical_facts":{"dc:creator":["Watt, Paul William"],"dc:date.accessioned":["2024-08-15T20:13:35Z"],"dc:date.available":["2024-08-15T20:13:35Z"],"dc:date.issued":["1982"],"dc:description.abstract":["Ribosomes are believed to be composed of many structurally and functionally important, protein-protein and RNA-protein domains. Two of these domains have been investigated. These are the 5S RNA-protein domain and the ribosomal 'A' protein domain. (i) An attempt has been made to isolate the 5S RNA-protein domain from the large ribosomal subunit of the eubacterium Escherichia coli, as the first step in a project to isolate this domain from an archaebacterial source. E. coli 50S subunits were subjected to a low concentration of Mg²⁺ (2 mM), EDTA•Na₂(10 mM) and NH₄Cl (1 M), (A. Liljas, unpublished), as a possible method to remove the 5S RNA­ protein complex from the ribosome. The suspension was centrifuged at 35,000 rpm for 15 hours in a Beckman Ti60 rotor and the supernatant obtained was passed through a 5-20% sucrose gradient. A fraction was obtained which contained several r-proteins and 5S RNA. In an attempt to purify the complex. further, the fraction was passed through an S200 column. Although evidence suggests that a complex was obtained, attempts to identify the composition were not successful. (ii) An attempt was also made to isolate the ribosomal 'A' protein domain, (equivalent to EL7/EL12-EL10 from E. coli), from the large subunit of wheat germ ribosomes, and to isolate and characterize its individual components. A putative complex has been found , of molecular weight 58, 000, containing three r-proteins with molecular weights 15, 000, 13, 700 and 32, 000 respectively. The N-terminal portions of each of these r-proteins has been sequenced. One protein (protein 8) was identified by its sequence as the ribosomal 'A' protein , while another (protein 7) has no homology with the N-terminal portion to protein 8. The third protein (protein 10) has been obtained and differs substantially from the other two proteins in molecular weight, but shows an identical N-terminal amino acid sequence to protein 7."],"dc:identifier.uri":["https://hdl.handle.net/1828/20060"],"dc:rights":["Available to the World Wide Web"],"dc:title":["Isolation and characterization of certain ribosomal domains : the 5S RNA-protein domain from Escherichia coli and the 'A' protein domain from wheat germ"],"dc:type":["Thesis"]},"updated_at":"2026-08-21T16:50:31Z"}