Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity
A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This partic...
Gespeichert in:
Veröffentlicht in: | The EMBO journal 1982-01, Vol.1 (5), p.609-613 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 613 |
---|---|
container_issue | 5 |
container_start_page | 609 |
container_title | The EMBO journal |
container_volume | 1 |
creator | Schulze, H. Nierhaus, K.H. |
description | A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This particle contains only 16 out of the 34 distinct components constituting the native subunit, and yet still exhibits significant PTF activity. Single omission tests at the level of this “minimal ribosomal particle” indicate the limits set on a further reduction of the components, and in particular reveal that protein L18 can be excluded from the set of proteins which are essential for PTF activity, thus leaving L2, L3, L4, L15, and L16 as primary candidates for this function. 5S RNA is not needed for PTF activity of the “minimal ribosomal particle”. Furthermore, a buffer condition is described which drastically improves the stability of total protein preparations and facilitates the isolation of individual proteins. |
doi_str_mv | 10.1002/j.1460-2075.1982.tb01216.x |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_553095</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15531712</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5756-6f39f971f07d176730f6fbdf9fad0c4ce69f4bd00f1e57d2e2c1108684fd044a3</originalsourceid><addsrcrecordid>eNqVkU1P3DAQhi1URLe0PwEp4tBb0hknthOkHiiCtgjEpb30YjmOXbzKxqntpey_J-muVuWEOHnk90Mzegg5RSgQgH5aFlhxyCkIVmBT0yK1gBR58XhAFnvpDVkA5ZhXWDdvybsYlwDAaoFH5IgLzmhJF-TXrRvcSvVZNCnzNguu9dHPH9qvRj-YIcXM-pAFo_0Qk0vr5PwwW9O9yUYzJtdt-hTUEK0JKppM6eQeXNq8J4dW9dF82L3H5OfV5Y-Lb_nN3dfvF-c3uWaC8ZzbsrGNQAuiQ8FFCZbbtrONVR3oShve2KrtACwaJjpqqEaEmteV7aCqVHlMPm97x3W7Mp2eVg6ql2OY7gob6ZWTz5XB3cvf_kEyVkLDpvzHXT74P2sTk1y5qE3fq8H4dZQ1lDVvSnjRiFMhCqST8Wxr1MHHGIzdL4MgZ4JyKWdMcsYkZ4JyR1A-TuGT_8_ZR3fIJv18q_91vdm8olle3n65_jeXT55Jr68</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15531712</pqid></control><display><type>article</type><title>Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Schulze, H. ; Nierhaus, K.H.</creator><creatorcontrib>Schulze, H. ; Nierhaus, K.H.</creatorcontrib><description>A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This particle contains only 16 out of the 34 distinct components constituting the native subunit, and yet still exhibits significant PTF activity. Single omission tests at the level of this “minimal ribosomal particle” indicate the limits set on a further reduction of the components, and in particular reveal that protein L18 can be excluded from the set of proteins which are essential for PTF activity, thus leaving L2, L3, L4, L15, and L16 as primary candidates for this function. 5S RNA is not needed for PTF activity of the “minimal ribosomal particle”. Furthermore, a buffer condition is described which drastically improves the stability of total protein preparations and facilitates the isolation of individual proteins.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1982.tb01216.x</identifier><identifier>PMID: 6765232</identifier><language>eng</language><publisher>England</publisher><subject>Acyltransferases - metabolism ; Escherichia coli ; Escherichia coli - enzymology ; Peptidyl Transferases - metabolism ; Ribosomal Proteins - isolation & purification ; Ribosomal Proteins - metabolism ; Ribosomes - enzymology ; Ribosomes - ultrastructure</subject><ispartof>The EMBO journal, 1982-01, Vol.1 (5), p.609-613</ispartof><rights>1982 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5756-6f39f971f07d176730f6fbdf9fad0c4ce69f4bd00f1e57d2e2c1108684fd044a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC553095/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC553095/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6765232$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schulze, H.</creatorcontrib><creatorcontrib>Nierhaus, K.H.</creatorcontrib><title>Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This particle contains only 16 out of the 34 distinct components constituting the native subunit, and yet still exhibits significant PTF activity. Single omission tests at the level of this “minimal ribosomal particle” indicate the limits set on a further reduction of the components, and in particular reveal that protein L18 can be excluded from the set of proteins which are essential for PTF activity, thus leaving L2, L3, L4, L15, and L16 as primary candidates for this function. 5S RNA is not needed for PTF activity of the “minimal ribosomal particle”. Furthermore, a buffer condition is described which drastically improves the stability of total protein preparations and facilitates the isolation of individual proteins.</description><subject>Acyltransferases - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Peptidyl Transferases - metabolism</subject><subject>Ribosomal Proteins - isolation & purification</subject><subject>Ribosomal Proteins - metabolism</subject><subject>Ribosomes - enzymology</subject><subject>Ribosomes - ultrastructure</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkU1P3DAQhi1URLe0PwEp4tBb0hknthOkHiiCtgjEpb30YjmOXbzKxqntpey_J-muVuWEOHnk90Mzegg5RSgQgH5aFlhxyCkIVmBT0yK1gBR58XhAFnvpDVkA5ZhXWDdvybsYlwDAaoFH5IgLzmhJF-TXrRvcSvVZNCnzNguu9dHPH9qvRj-YIcXM-pAFo_0Qk0vr5PwwW9O9yUYzJtdt-hTUEK0JKppM6eQeXNq8J4dW9dF82L3H5OfV5Y-Lb_nN3dfvF-c3uWaC8ZzbsrGNQAuiQ8FFCZbbtrONVR3oShve2KrtACwaJjpqqEaEmteV7aCqVHlMPm97x3W7Mp2eVg6ql2OY7gob6ZWTz5XB3cvf_kEyVkLDpvzHXT74P2sTk1y5qE3fq8H4dZQ1lDVvSnjRiFMhCqST8Wxr1MHHGIzdL4MgZ4JyKWdMcsYkZ4JyR1A-TuGT_8_ZR3fIJv18q_91vdm8olle3n65_jeXT55Jr68</recordid><startdate>19820101</startdate><enddate>19820101</enddate><creator>Schulze, H.</creator><creator>Nierhaus, K.H.</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19820101</creationdate><title>Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity</title><author>Schulze, H. ; Nierhaus, K.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5756-6f39f971f07d176730f6fbdf9fad0c4ce69f4bd00f1e57d2e2c1108684fd044a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Acyltransferases - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Peptidyl Transferases - metabolism</topic><topic>Ribosomal Proteins - isolation & purification</topic><topic>Ribosomal Proteins - metabolism</topic><topic>Ribosomes - enzymology</topic><topic>Ribosomes - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schulze, H.</creatorcontrib><creatorcontrib>Nierhaus, K.H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schulze, H.</au><au>Nierhaus, K.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1982-01-01</date><risdate>1982</risdate><volume>1</volume><issue>5</issue><spage>609</spage><epage>613</epage><pages>609-613</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This particle contains only 16 out of the 34 distinct components constituting the native subunit, and yet still exhibits significant PTF activity. Single omission tests at the level of this “minimal ribosomal particle” indicate the limits set on a further reduction of the components, and in particular reveal that protein L18 can be excluded from the set of proteins which are essential for PTF activity, thus leaving L2, L3, L4, L15, and L16 as primary candidates for this function. 5S RNA is not needed for PTF activity of the “minimal ribosomal particle”. Furthermore, a buffer condition is described which drastically improves the stability of total protein preparations and facilitates the isolation of individual proteins.</abstract><cop>England</cop><pmid>6765232</pmid><doi>10.1002/j.1460-2075.1982.tb01216.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0261-4189 |
ispartof | The EMBO journal, 1982-01, Vol.1 (5), p.609-613 |
issn | 0261-4189 1460-2075 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_553095 |
source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | Acyltransferases - metabolism Escherichia coli Escherichia coli - enzymology Peptidyl Transferases - metabolism Ribosomal Proteins - isolation & purification Ribosomal Proteins - metabolism Ribosomes - enzymology Ribosomes - ultrastructure |
title | Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T16%3A59%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Minimal%20set%20of%20ribosomal%20components%20for%20reconstitution%20of%20the%20peptidyltransferase%20activity&rft.jtitle=The%20EMBO%20journal&rft.au=Schulze,%20H.&rft.date=1982-01-01&rft.volume=1&rft.issue=5&rft.spage=609&rft.epage=613&rft.pages=609-613&rft.issn=0261-4189&rft.eissn=1460-2075&rft_id=info:doi/10.1002/j.1460-2075.1982.tb01216.x&rft_dat=%3Cproquest_pubme%3E15531712%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15531712&rft_id=info:pmid/6765232&rfr_iscdi=true |