Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form
A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in s...
Gespeichert in:
| Veröffentlicht in: | Cell 2002-11, Vol.111 (5), p.721-732 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 732 |
|---|---|
| container_issue | 5 |
| container_start_page | 721 |
| container_title | Cell |
| container_volume | 111 |
| creator | Ogle, James M. Murphy, Frank V. Tarry, Michael J. Ramakrishnan, V. |
| description | A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity. |
| doi_str_mv | 10.1016/S0092-8674(02)01086-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72741419</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0092867402010863</els_id><sourcerecordid>18651863</sourcerecordid><originalsourceid>FETCH-LOGICAL-c557t-a66425b0fdf152bc2cf2a0c24aa5b9457f19571f6ebd6507b5952dfb491039f13</originalsourceid><addsrcrecordid>eNqFkE1r3DAQhkVpabZJfkKDTiU5uNXI-rBPYVmSNhAayMdZSPKIqtjWRvIG8u_j_aA95jDMwDwzLzyEfAX2HRioHw-MtbxqlBbnjF8wYI2q6g9kAazVlQDNP5LFP-SIfCnlL2OskVJ-JkfAhRLQ1Avy9IA9-immkaZAp_vfS-pe6fQH6X10qaRhHvB5EzMWauljtmOJOzrkNFA70rs1jnRK83LVp4IdvU55OCGfgu0Lnh76MXm6vnpc_apu737erJa3lZdST5VVSnDpWOgCSO4894Fb5rmwVrpWSB2glRqCQtcpybSTreRdcKIFVrcB6mPybf93ndPzBstkhlg89r0dMW2K0VwLENC-C0Kj5Fz1DMo96HMqJWMw6xwHm18NMLMVb3bizdaqYdzsxJvt3dkhYOMG7P5fHUzPwOUewNnHS8Rsio84euxmt34yXYrvRLwBX-SQ4w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18651863</pqid></control><display><type>article</type><title>Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Cell Press Free Archives</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Ogle, James M. ; Murphy, Frank V. ; Tarry, Michael J. ; Ramakrishnan, V.</creator><creatorcontrib>Ogle, James M. ; Murphy, Frank V. ; Tarry, Michael J. ; Ramakrishnan, V.</creatorcontrib><description>A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(02)01086-3</identifier><identifier>PMID: 12464183</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anti-Bacterial Agents - metabolism ; Anti-Bacterial Agents - pharmacology ; Anticodon - chemistry ; Anticodon - metabolism ; Base Pairing ; Binding, Competitive ; Codon - chemistry ; Codon - metabolism ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Paromomycin - metabolism ; Paromomycin - pharmacology ; Ribosomes - chemistry ; Ribosomes - metabolism ; RNA, Bacterial - chemistry ; RNA, Bacterial - metabolism ; RNA, Ribosomal, 16S - chemistry ; RNA, Ribosomal, 16S - metabolism ; RNA, Transfer - chemistry ; RNA, Transfer - metabolism ; RNA, Transfer, Phe - chemistry ; RNA, Transfer, Phe - metabolism ; Structure-Activity Relationship ; Thermodynamics ; Thermus thermophilus</subject><ispartof>Cell, 2002-11, Vol.111 (5), p.721-732</ispartof><rights>2002 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-a66425b0fdf152bc2cf2a0c24aa5b9457f19571f6ebd6507b5952dfb491039f13</citedby><cites>FETCH-LOGICAL-c557t-a66425b0fdf152bc2cf2a0c24aa5b9457f19571f6ebd6507b5952dfb491039f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867402010863$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12464183$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogle, James M.</creatorcontrib><creatorcontrib>Murphy, Frank V.</creatorcontrib><creatorcontrib>Tarry, Michael J.</creatorcontrib><creatorcontrib>Ramakrishnan, V.</creatorcontrib><title>Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form</title><title>Cell</title><addtitle>Cell</addtitle><description>A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity.</description><subject>Anti-Bacterial Agents - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Anticodon - chemistry</subject><subject>Anticodon - metabolism</subject><subject>Base Pairing</subject><subject>Binding, Competitive</subject><subject>Codon - chemistry</subject><subject>Codon - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Hydrogen Bonding</subject><subject>Models, Molecular</subject><subject>Nucleic Acid Conformation</subject><subject>Paromomycin - metabolism</subject><subject>Paromomycin - pharmacology</subject><subject>Ribosomes - chemistry</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Bacterial - chemistry</subject><subject>RNA, Bacterial - metabolism</subject><subject>RNA, Ribosomal, 16S - chemistry</subject><subject>RNA, Ribosomal, 16S - metabolism</subject><subject>RNA, Transfer - chemistry</subject><subject>RNA, Transfer - metabolism</subject><subject>RNA, Transfer, Phe - chemistry</subject><subject>RNA, Transfer, Phe - metabolism</subject><subject>Structure-Activity Relationship</subject><subject>Thermodynamics</subject><subject>Thermus thermophilus</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVpabZJfkKDTiU5uNXI-rBPYVmSNhAayMdZSPKIqtjWRvIG8u_j_aA95jDMwDwzLzyEfAX2HRioHw-MtbxqlBbnjF8wYI2q6g9kAazVlQDNP5LFP-SIfCnlL2OskVJ-JkfAhRLQ1Avy9IA9-immkaZAp_vfS-pe6fQH6X10qaRhHvB5EzMWauljtmOJOzrkNFA70rs1jnRK83LVp4IdvU55OCGfgu0Lnh76MXm6vnpc_apu737erJa3lZdST5VVSnDpWOgCSO4894Fb5rmwVrpWSB2glRqCQtcpybSTreRdcKIFVrcB6mPybf93ndPzBstkhlg89r0dMW2K0VwLENC-C0Kj5Fz1DMo96HMqJWMw6xwHm18NMLMVb3bizdaqYdzsxJvt3dkhYOMG7P5fHUzPwOUewNnHS8Rsio84euxmt34yXYrvRLwBX-SQ4w</recordid><startdate>20021127</startdate><enddate>20021127</enddate><creator>Ogle, James M.</creator><creator>Murphy, Frank V.</creator><creator>Tarry, Michael J.</creator><creator>Ramakrishnan, V.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20021127</creationdate><title>Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form</title><author>Ogle, James M. ; Murphy, Frank V. ; Tarry, Michael J. ; Ramakrishnan, V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-a66425b0fdf152bc2cf2a0c24aa5b9457f19571f6ebd6507b5952dfb491039f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Anti-Bacterial Agents - metabolism</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Anticodon - chemistry</topic><topic>Anticodon - metabolism</topic><topic>Base Pairing</topic><topic>Binding, Competitive</topic><topic>Codon - chemistry</topic><topic>Codon - metabolism</topic><topic>Crystallography, X-Ray</topic><topic>Hydrogen Bonding</topic><topic>Models, Molecular</topic><topic>Nucleic Acid Conformation</topic><topic>Paromomycin - metabolism</topic><topic>Paromomycin - pharmacology</topic><topic>Ribosomes - chemistry</topic><topic>Ribosomes - metabolism</topic><topic>RNA, Bacterial - chemistry</topic><topic>RNA, Bacterial - metabolism</topic><topic>RNA, Ribosomal, 16S - chemistry</topic><topic>RNA, Ribosomal, 16S - metabolism</topic><topic>RNA, Transfer - chemistry</topic><topic>RNA, Transfer - metabolism</topic><topic>RNA, Transfer, Phe - chemistry</topic><topic>RNA, Transfer, Phe - metabolism</topic><topic>Structure-Activity Relationship</topic><topic>Thermodynamics</topic><topic>Thermus thermophilus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogle, James M.</creatorcontrib><creatorcontrib>Murphy, Frank V.</creatorcontrib><creatorcontrib>Tarry, Michael J.</creatorcontrib><creatorcontrib>Ramakrishnan, V.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogle, James M.</au><au>Murphy, Frank V.</au><au>Tarry, Michael J.</au><au>Ramakrishnan, V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2002-11-27</date><risdate>2002</risdate><volume>111</volume><issue>5</issue><spage>721</spage><epage>732</epage><pages>721-732</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12464183</pmid><doi>10.1016/S0092-8674(02)01086-3</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 2002-11, Vol.111 (5), p.721-732 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72741419 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals |
| subjects | Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Anticodon - chemistry Anticodon - metabolism Base Pairing Binding, Competitive Codon - chemistry Codon - metabolism Crystallography, X-Ray Hydrogen Bonding Models, Molecular Nucleic Acid Conformation Paromomycin - metabolism Paromomycin - pharmacology Ribosomes - chemistry Ribosomes - metabolism RNA, Bacterial - chemistry RNA, Bacterial - metabolism RNA, Ribosomal, 16S - chemistry RNA, Ribosomal, 16S - metabolism RNA, Transfer - chemistry RNA, Transfer - metabolism RNA, Transfer, Phe - chemistry RNA, Transfer, Phe - metabolism Structure-Activity Relationship Thermodynamics Thermus thermophilus |
| title | Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T18%3A45%3A22IST&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=Selection%20of%20tRNA%20by%20the%20Ribosome%20Requires%20a%20Transition%20from%20an%20Open%20to%20a%20Closed%20Form&rft.jtitle=Cell&rft.au=Ogle,%20James%20M.&rft.date=2002-11-27&rft.volume=111&rft.issue=5&rft.spage=721&rft.epage=732&rft.pages=721-732&rft.issn=0092-8674&rft.eissn=1097-4172&rft_id=info:doi/10.1016/S0092-8674(02)01086-3&rft_dat=%3Cproquest_cross%3E18651863%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=18651863&rft_id=info:pmid/12464183&rft_els_id=S0092867402010863&rfr_iscdi=true |