Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro
Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit...
Gespeichert in:
| Veröffentlicht in: | European journal of biochemistry 1980, Vol.107 (1), p.95-103 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 103 |
|---|---|
| container_issue | 1 |
| container_start_page | 95 |
| container_title | European journal of biochemistry |
| container_volume | 107 |
| creator | Hayes, F Schmitt, S |
| description | Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit proteins of either strain are used even at temperatures which are not permissive for 30-S subunit assembly in vivo in E. coli 219ts2. The yield of reconstitution is, however, twofold lower with 30-S subunit proteins of E. coli 219ts2 than with wild-type proteins. 2. The yield of complex formation between 16-S rRNA and protein S4 of E. coli 219ts2 is temperature-sensitive and lower at all temperatures tested (33-42 degrees C) than that observed when wild-type S4 is used. 3. The conformational stability of complexes between 16-S rRNA and S4 from 219ts2 is more temperature-sensitive than that of analogous complexes containing wild-type S4. These observations provide an explanation for the temperature sensitivity of 30-S subunit assembly in E. coli 219ts2. |
| doi_str_mv | 10.1111/j.1432-1033.1980.tb04629.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75196264</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>75196264</sourcerecordid><originalsourceid>FETCH-LOGICAL-c172t-9c077bed97a6e22207a495c633cbf1ec189550604929fb8b8dbb120c54f2ee633</originalsourceid><addsrcrecordid>eNo9kMtOwzAQRS0EKuXxCUgWC3YJtpM4MTsE5SEhsYG1ZbsT1VUexeOgdsG_k9CK2cxIc--d0SHkmrOUj3W7TnmeiYSzLEu5qlgaLculUOn2iMz_V8dkzhjPE6EKeUrOENeMMalkOSMzqVTBeTUnP49Qg4v-G6hBhNY2O9rXNK6AYmuahgZve-zHkeJgh85H6jtqaIR2A8HEIUCC0KH_i2iHaLo4BSzQrSB4t_KGur7xKV1sR4NvoYs4RXz7GPoLclKbBuHy0M_J59Pi4-EleXt_fn24f0scL0VMlGNlaWGpSiNBCMFKk6vCySxztubgeKWKgkmWK6FqW9lqaS0XzBV5LQBG2Tm52eduQv81AEbdenTQNKaDfkBdFlxJIfNReLcXutAjBqj1ZvzZhJ3mTE_s9VpPgPUEWE_s9YG93o7mq8OVwbaw_LceYGe_CVqD0Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>75196264</pqid></control><display><type>article</type><title>Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Hayes, F ; Schmitt, S</creator><creatorcontrib>Hayes, F ; Schmitt, S</creatorcontrib><description>Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit proteins of either strain are used even at temperatures which are not permissive for 30-S subunit assembly in vivo in E. coli 219ts2. The yield of reconstitution is, however, twofold lower with 30-S subunit proteins of E. coli 219ts2 than with wild-type proteins. 2. The yield of complex formation between 16-S rRNA and protein S4 of E. coli 219ts2 is temperature-sensitive and lower at all temperatures tested (33-42 degrees C) than that observed when wild-type S4 is used. 3. The conformational stability of complexes between 16-S rRNA and S4 from 219ts2 is more temperature-sensitive than that of analogous complexes containing wild-type S4. These observations provide an explanation for the temperature sensitivity of 30-S subunit assembly in E. coli 219ts2.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1980.tb04629.x</identifier><identifier>PMID: 6995118</identifier><language>eng</language><publisher>England</publisher><subject>Chromatography, Gel ; Escherichia coli - metabolism ; Macromolecular Substances ; Molecular Weight ; Mutation ; Protein Conformation ; Ribosomal Proteins - isolation & purification ; Ribosomal Proteins - metabolism ; Ribosomes - metabolism ; Ribosomes - ultrastructure ; Temperature</subject><ispartof>European journal of biochemistry, 1980, Vol.107 (1), p.95-103</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c172t-9c077bed97a6e22207a495c633cbf1ec189550604929fb8b8dbb120c54f2ee633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6995118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hayes, F</creatorcontrib><creatorcontrib>Schmitt, S</creatorcontrib><title>Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit proteins of either strain are used even at temperatures which are not permissive for 30-S subunit assembly in vivo in E. coli 219ts2. The yield of reconstitution is, however, twofold lower with 30-S subunit proteins of E. coli 219ts2 than with wild-type proteins. 2. The yield of complex formation between 16-S rRNA and protein S4 of E. coli 219ts2 is temperature-sensitive and lower at all temperatures tested (33-42 degrees C) than that observed when wild-type S4 is used. 3. The conformational stability of complexes between 16-S rRNA and S4 from 219ts2 is more temperature-sensitive than that of analogous complexes containing wild-type S4. These observations provide an explanation for the temperature sensitivity of 30-S subunit assembly in E. coli 219ts2.</description><subject>Chromatography, Gel</subject><subject>Escherichia coli - metabolism</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>Ribosomal Proteins - isolation & purification</subject><subject>Ribosomal Proteins - metabolism</subject><subject>Ribosomes - metabolism</subject><subject>Ribosomes - ultrastructure</subject><subject>Temperature</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtOwzAQRS0EKuXxCUgWC3YJtpM4MTsE5SEhsYG1ZbsT1VUexeOgdsG_k9CK2cxIc--d0SHkmrOUj3W7TnmeiYSzLEu5qlgaLculUOn2iMz_V8dkzhjPE6EKeUrOENeMMalkOSMzqVTBeTUnP49Qg4v-G6hBhNY2O9rXNK6AYmuahgZve-zHkeJgh85H6jtqaIR2A8HEIUCC0KH_i2iHaLo4BSzQrSB4t_KGur7xKV1sR4NvoYs4RXz7GPoLclKbBuHy0M_J59Pi4-EleXt_fn24f0scL0VMlGNlaWGpSiNBCMFKk6vCySxztubgeKWKgkmWK6FqW9lqaS0XzBV5LQBG2Tm52eduQv81AEbdenTQNKaDfkBdFlxJIfNReLcXutAjBqj1ZvzZhJ3mTE_s9VpPgPUEWE_s9YG93o7mq8OVwbaw_LceYGe_CVqD0Q</recordid><startdate>1980</startdate><enddate>1980</enddate><creator>Hayes, F</creator><creator>Schmitt, S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1980</creationdate><title>Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro</title><author>Hayes, F ; Schmitt, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c172t-9c077bed97a6e22207a495c633cbf1ec189550604929fb8b8dbb120c54f2ee633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Chromatography, Gel</topic><topic>Escherichia coli - metabolism</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>Ribosomal Proteins - isolation & purification</topic><topic>Ribosomal Proteins - metabolism</topic><topic>Ribosomes - metabolism</topic><topic>Ribosomes - ultrastructure</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hayes, F</creatorcontrib><creatorcontrib>Schmitt, S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hayes, F</au><au>Schmitt, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1980</date><risdate>1980</risdate><volume>107</volume><issue>1</issue><spage>95</spage><epage>103</epage><pages>95-103</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit proteins of either strain are used even at temperatures which are not permissive for 30-S subunit assembly in vivo in E. coli 219ts2. The yield of reconstitution is, however, twofold lower with 30-S subunit proteins of E. coli 219ts2 than with wild-type proteins. 2. The yield of complex formation between 16-S rRNA and protein S4 of E. coli 219ts2 is temperature-sensitive and lower at all temperatures tested (33-42 degrees C) than that observed when wild-type S4 is used. 3. The conformational stability of complexes between 16-S rRNA and S4 from 219ts2 is more temperature-sensitive than that of analogous complexes containing wild-type S4. These observations provide an explanation for the temperature sensitivity of 30-S subunit assembly in E. coli 219ts2.</abstract><cop>England</cop><pmid>6995118</pmid><doi>10.1111/j.1432-1033.1980.tb04629.x</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1980, Vol.107 (1), p.95-103 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75196264 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Chromatography, Gel Escherichia coli - metabolism Macromolecular Substances Molecular Weight Mutation Protein Conformation Ribosomal Proteins - isolation & purification Ribosomal Proteins - metabolism Ribosomes - metabolism Ribosomes - ultrastructure Temperature |
| title | Defective assembly of the small ribosomal subunit in a temperature-sensitive mutant of Escherichia coli. Experiments in vitro |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T04%3A23%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Defective%20assembly%20of%20the%20small%20ribosomal%20subunit%20in%20a%20temperature-sensitive%20mutant%20of%20Escherichia%20coli.%20Experiments%20in%20vitro&rft.jtitle=European%20journal%20of%20biochemistry&rft.au=Hayes,%20F&rft.date=1980&rft.volume=107&rft.issue=1&rft.spage=95&rft.epage=103&rft.pages=95-103&rft.issn=0014-2956&rft.eissn=1432-1033&rft_id=info:doi/10.1111/j.1432-1033.1980.tb04629.x&rft_dat=%3Cproquest_cross%3E75196264%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=75196264&rft_id=info:pmid/6995118&rfr_iscdi=true |