Assembly in Vitro of the 50 S subunit from Escherichia coli ribosomes: Proteins essential for the first heat-dependent conformational change
An early intermediate during the assembly in vitro of the ribosomal 50 S subunit is the RI 50(1) particle, which undergoes a drastic change in s value to form the RI 50 ∗(1) particle. The formation of this RI 50 ∗(1) particle, which is essential for the assembly of a highly active 50 S particle, was...
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| Veröffentlicht in: | Journal of molecular biology 1977-09, Vol.115 (3), p.513-523 |
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| container_title | Journal of molecular biology |
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| creator | Spillmann, Susanne Dohme, Ferdinand Nierhaus, Knud H. |
| description | An early intermediate during the assembly
in vitro of the ribosomal 50 S subunit is the RI
50(1) particle, which undergoes a drastic change in
s value to form the RI
50
∗(1) particle. The formation of this RI
50
∗(1) particle, which is essential for the assembly of a highly active 50 S particle, was analyzed. Total reconstitution experiments with purified proteins revealed that six ribosomal components (23 S RNA and the proteins L4, L13, L20, L22 and L24) are essential for the RI
50
∗(1) formation. Protein L3 had a stimulatory effect, but was not essential. With these seven components, a particle with the RI
50
∗ conformation could be formed.
A comparison with assembly
in vivo demonstrated that the pathways of protein assembly
in vitro and
in vivo are very similar at the beginning, but diverge towards the end of the process. Furthermore, the sequence in which the proteins can be split off the 50 S subunit by increasing concentrations of LiCl corresponds, to a first approximation, to the reverse of the order of assembly
in vitro. |
| doi_str_mv | 10.1016/0022-2836(77)90168-1 |
| format | Article |
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in vitro of the ribosomal 50 S subunit is the RI
50(1) particle, which undergoes a drastic change in
s value to form the RI
50
∗(1) particle. The formation of this RI
50
∗(1) particle, which is essential for the assembly of a highly active 50 S particle, was analyzed. Total reconstitution experiments with purified proteins revealed that six ribosomal components (23 S RNA and the proteins L4, L13, L20, L22 and L24) are essential for the RI
50
∗(1) formation. Protein L3 had a stimulatory effect, but was not essential. With these seven components, a particle with the RI
50
∗ conformation could be formed.
A comparison with assembly
in vivo demonstrated that the pathways of protein assembly
in vitro and
in vivo are very similar at the beginning, but diverge towards the end of the process. Furthermore, the sequence in which the proteins can be split off the 50 S subunit by increasing concentrations of LiCl corresponds, to a first approximation, to the reverse of the order of assembly
in vitro.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(77)90168-1</identifier><identifier>PMID: 338913</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Escherichia coli - metabolism ; Molecular Weight ; Nucleic Acid Conformation ; Ribosomal Proteins - metabolism ; Ribosomes - metabolism ; RNA, Ribosomal - biosynthesis</subject><ispartof>Journal of molecular biology, 1977-09, Vol.115 (3), p.513-523</ispartof><rights>1977</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c271t-d3fcaac75b8f369550b7639118edae3d40b89e37fbdaf185fd37cf636d4e5f633</citedby><cites>FETCH-LOGICAL-c271t-d3fcaac75b8f369550b7639118edae3d40b89e37fbdaf185fd37cf636d4e5f633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0022283677901681$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/338913$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Spillmann, Susanne</creatorcontrib><creatorcontrib>Dohme, Ferdinand</creatorcontrib><creatorcontrib>Nierhaus, Knud H.</creatorcontrib><title>Assembly in Vitro of the 50 S subunit from Escherichia coli ribosomes: Proteins essential for the first heat-dependent conformational change</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>An early intermediate during the assembly
in vitro of the ribosomal 50 S subunit is the RI
50(1) particle, which undergoes a drastic change in
s value to form the RI
50
∗(1) particle. The formation of this RI
50
∗(1) particle, which is essential for the assembly of a highly active 50 S particle, was analyzed. Total reconstitution experiments with purified proteins revealed that six ribosomal components (23 S RNA and the proteins L4, L13, L20, L22 and L24) are essential for the RI
50
∗(1) formation. Protein L3 had a stimulatory effect, but was not essential. With these seven components, a particle with the RI
50
∗ conformation could be formed.
A comparison with assembly
in vivo demonstrated that the pathways of protein assembly
in vitro and
in vivo are very similar at the beginning, but diverge towards the end of the process. Furthermore, the sequence in which the proteins can be split off the 50 S subunit by increasing concentrations of LiCl corresponds, to a first approximation, to the reverse of the order of assembly
in vitro.</description><subject>Escherichia coli - metabolism</subject><subject>Molecular Weight</subject><subject>Nucleic Acid Conformation</subject><subject>Ribosomal Proteins - metabolism</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Ribosomal - biosynthesis</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9rFTEUxYP471n9Bl1kJXYxNXmZmWRcFEpptVCwUHUbMsmNE5lJnrkZod_BD21eX-nS1YV7zvnBPZeQY85OOeP9R8a222arRP9BypOhblTDn5ENZ2poVC_Uc7J5srwmbxB_McY60apX5KUQauBiQ_6eI8Iyzvc0RPojlJxo8rRMQDtG7yiu4xpDoT6nhV6inSAHOwVDbZoDzWFMmBbAT_Q2pwIhIoXKiyWYmfqUH0A-ZCx0AlMaBzuIruo1H6u-mBJSrF47mfgT3pIX3swI7x7nEfl-dfnt4ktz8_Xz9cX5TWO3kleK8NYYK7tRedEPXcdG2YuBcwXOgHAtG9UAQvrRGc9V552Q1veidy10dYoj8v7A3eX0ewUsegloYZ5NhLSilkLyfmiHamwPRpsTYgavdzksJt9rzvT-B3pfsN4XrKXUDz_QvMaOH_nruIB7Ch1Kr_LZQYZ6458AWaMNEC24kMEW7VL4P_8fBw-YfA</recordid><startdate>19770925</startdate><enddate>19770925</enddate><creator>Spillmann, Susanne</creator><creator>Dohme, Ferdinand</creator><creator>Nierhaus, Knud H.</creator><general>Elsevier Ltd</general><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>19770925</creationdate><title>Assembly in Vitro of the 50 S subunit from Escherichia coli ribosomes: Proteins essential for the first heat-dependent conformational change</title><author>Spillmann, Susanne ; Dohme, Ferdinand ; Nierhaus, Knud H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c271t-d3fcaac75b8f369550b7639118edae3d40b89e37fbdaf185fd37cf636d4e5f633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Escherichia coli - metabolism</topic><topic>Molecular Weight</topic><topic>Nucleic Acid Conformation</topic><topic>Ribosomal Proteins - metabolism</topic><topic>Ribosomes - metabolism</topic><topic>RNA, Ribosomal - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spillmann, Susanne</creatorcontrib><creatorcontrib>Dohme, Ferdinand</creatorcontrib><creatorcontrib>Nierhaus, Knud 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>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Spillmann, Susanne</au><au>Dohme, Ferdinand</au><au>Nierhaus, Knud H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Assembly in Vitro of the 50 S subunit from Escherichia coli ribosomes: Proteins essential for the first heat-dependent conformational change</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1977-09-25</date><risdate>1977</risdate><volume>115</volume><issue>3</issue><spage>513</spage><epage>523</epage><pages>513-523</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>An early intermediate during the assembly
in vitro of the ribosomal 50 S subunit is the RI
50(1) particle, which undergoes a drastic change in
s value to form the RI
50
∗(1) particle. The formation of this RI
50
∗(1) particle, which is essential for the assembly of a highly active 50 S particle, was analyzed. Total reconstitution experiments with purified proteins revealed that six ribosomal components (23 S RNA and the proteins L4, L13, L20, L22 and L24) are essential for the RI
50
∗(1) formation. Protein L3 had a stimulatory effect, but was not essential. With these seven components, a particle with the RI
50
∗ conformation could be formed.
A comparison with assembly
in vivo demonstrated that the pathways of protein assembly
in vitro and
in vivo are very similar at the beginning, but diverge towards the end of the process. Furthermore, the sequence in which the proteins can be split off the 50 S subunit by increasing concentrations of LiCl corresponds, to a first approximation, to the reverse of the order of assembly
in vitro.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>338913</pmid><doi>10.1016/0022-2836(77)90168-1</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1977-09, Vol.115 (3), p.513-523 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73716949 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Escherichia coli - metabolism Molecular Weight Nucleic Acid Conformation Ribosomal Proteins - metabolism Ribosomes - metabolism RNA, Ribosomal - biosynthesis |
| title | Assembly in Vitro of the 50 S subunit from Escherichia coli ribosomes: Proteins essential for the first heat-dependent conformational change |
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