Ribonuclease P: a ribonucleoprotein enzyme
The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5′ end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA–P-protein and RNase-P-RNA–precursor-tRNA complexes, as well as on the positions of cata...
Gespeichert in:
Veröffentlicht in: | Current Opinion in Chemical Biology 2000-10, Vol.4 (5), p.553-558 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 558 |
---|---|
container_issue | 5 |
container_start_page | 553 |
container_title | Current Opinion in Chemical Biology |
container_volume | 4 |
creator | Kurz, Jeffrey C Fierke, Carol A |
description | The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5′ end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA–P-protein and RNase-P-RNA–precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the structure to the catalytic function. |
doi_str_mv | 10.1016/S1367-5931(00)00131-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72304522</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1367593100001319</els_id><sourcerecordid>72304522</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-d8733be54d31dc4a957c4a791f36c2039c0a20e44d9314426b9e5338307496bb3</originalsourceid><addsrcrecordid>eNqFkNtKw0AQhhdRbK0-gpIrUSE6e856I1I8QUHxcL0kmymspEnNJkJ9ercH8bI3s8PyzfzDR8gxhUsKVF29Ua50Kg2nZwDnAJTT1OyQIc20SUEA2439HzIgByF8AoBimdwnA0pjK4UYkotXXzR17yrMAyYv10metH8_zbxtOvR1gvXPYoaHZG-aVwGPNu-IfNzfvY8f08nzw9P4dpI6bliXlpnmvEApSk5LJ3Ijdaza0ClXjgE3DnIGKEQZDxOCqcKg5DzjoIVRRcFH5HS9N8Z_9Rg6O_PBYVXlNTZ9sJpxEJKxrSDVimdCZRGUa9C1TQgtTu289bO8XVgKdmnTrmzapSoLYFc2rYlzJ5uAvphh-T-10ReBmzWA0ce3x9YG57F2WPoWXWfLxm-J-AUEZ4GE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17638468</pqid></control><display><type>article</type><title>Ribonuclease P: a ribonucleoprotein enzyme</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Kurz, Jeffrey C ; Fierke, Carol A</creator><creatorcontrib>Kurz, Jeffrey C ; Fierke, Carol A</creatorcontrib><description>The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5′ end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA–P-protein and RNase-P-RNA–precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the structure to the catalytic function.</description><identifier>ISSN: 1367-5931</identifier><identifier>EISSN: 1879-0402</identifier><identifier>DOI: 10.1016/S1367-5931(00)00131-9</identifier><identifier>PMID: 11006544</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Base Sequence ; Catalysis ; Endoribonucleases - chemistry ; Endoribonucleases - metabolism ; NAIM ; Nucleic Acid Conformation ; Ribonuclease P ; RNA, Catalytic - chemistry ; RNA, Catalytic - metabolism ; RNA, Transfer, Asp - chemistry ; RNA, Transfer, Asp - metabolism ; Substrate recognition ; Substrate Specificity ; tRNA</subject><ispartof>Current Opinion in Chemical Biology, 2000-10, Vol.4 (5), p.553-558</ispartof><rights>2000 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-d8733be54d31dc4a957c4a791f36c2039c0a20e44d9314426b9e5338307496bb3</citedby><cites>FETCH-LOGICAL-c392t-d8733be54d31dc4a957c4a791f36c2039c0a20e44d9314426b9e5338307496bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1367-5931(00)00131-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>313,314,777,781,789,3537,27903,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11006544$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kurz, Jeffrey C</creatorcontrib><creatorcontrib>Fierke, Carol A</creatorcontrib><title>Ribonuclease P: a ribonucleoprotein enzyme</title><title>Current Opinion in Chemical Biology</title><addtitle>Curr Opin Chem Biol</addtitle><description>The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5′ end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA–P-protein and RNase-P-RNA–precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the structure to the catalytic function.</description><subject>Base Sequence</subject><subject>Catalysis</subject><subject>Endoribonucleases - chemistry</subject><subject>Endoribonucleases - metabolism</subject><subject>NAIM</subject><subject>Nucleic Acid Conformation</subject><subject>Ribonuclease P</subject><subject>RNA, Catalytic - chemistry</subject><subject>RNA, Catalytic - metabolism</subject><subject>RNA, Transfer, Asp - chemistry</subject><subject>RNA, Transfer, Asp - metabolism</subject><subject>Substrate recognition</subject><subject>Substrate Specificity</subject><subject>tRNA</subject><issn>1367-5931</issn><issn>1879-0402</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkNtKw0AQhhdRbK0-gpIrUSE6e856I1I8QUHxcL0kmymspEnNJkJ9ercH8bI3s8PyzfzDR8gxhUsKVF29Ua50Kg2nZwDnAJTT1OyQIc20SUEA2439HzIgByF8AoBimdwnA0pjK4UYkotXXzR17yrMAyYv10metH8_zbxtOvR1gvXPYoaHZG-aVwGPNu-IfNzfvY8f08nzw9P4dpI6bliXlpnmvEApSk5LJ3Ijdaza0ClXjgE3DnIGKEQZDxOCqcKg5DzjoIVRRcFH5HS9N8Z_9Rg6O_PBYVXlNTZ9sJpxEJKxrSDVimdCZRGUa9C1TQgtTu289bO8XVgKdmnTrmzapSoLYFc2rYlzJ5uAvphh-T-10ReBmzWA0ce3x9YG57F2WPoWXWfLxm-J-AUEZ4GE</recordid><startdate>20001001</startdate><enddate>20001001</enddate><creator>Kurz, Jeffrey C</creator><creator>Fierke, Carol A</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20001001</creationdate><title>Ribonuclease P: a ribonucleoprotein enzyme</title><author>Kurz, Jeffrey C ; Fierke, Carol A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-d8733be54d31dc4a957c4a791f36c2039c0a20e44d9314426b9e5338307496bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Base Sequence</topic><topic>Catalysis</topic><topic>Endoribonucleases - chemistry</topic><topic>Endoribonucleases - metabolism</topic><topic>NAIM</topic><topic>Nucleic Acid Conformation</topic><topic>Ribonuclease P</topic><topic>RNA, Catalytic - chemistry</topic><topic>RNA, Catalytic - metabolism</topic><topic>RNA, Transfer, Asp - chemistry</topic><topic>RNA, Transfer, Asp - metabolism</topic><topic>Substrate recognition</topic><topic>Substrate Specificity</topic><topic>tRNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kurz, Jeffrey C</creatorcontrib><creatorcontrib>Fierke, Carol A</creatorcontrib><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>Current Opinion in Chemical Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kurz, Jeffrey C</au><au>Fierke, Carol A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ribonuclease P: a ribonucleoprotein enzyme</atitle><jtitle>Current Opinion in Chemical Biology</jtitle><addtitle>Curr Opin Chem Biol</addtitle><date>2000-10-01</date><risdate>2000</risdate><volume>4</volume><issue>5</issue><spage>553</spage><epage>558</epage><pages>553-558</pages><issn>1367-5931</issn><eissn>1879-0402</eissn><abstract>The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5′ end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA–P-protein and RNase-P-RNA–precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the structure to the catalytic function.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>11006544</pmid><doi>10.1016/S1367-5931(00)00131-9</doi><tpages>6</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1367-5931 |
ispartof | Current Opinion in Chemical Biology, 2000-10, Vol.4 (5), p.553-558 |
issn | 1367-5931 1879-0402 |
language | eng |
recordid | cdi_proquest_miscellaneous_72304522 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Base Sequence Catalysis Endoribonucleases - chemistry Endoribonucleases - metabolism NAIM Nucleic Acid Conformation Ribonuclease P RNA, Catalytic - chemistry RNA, Catalytic - metabolism RNA, Transfer, Asp - chemistry RNA, Transfer, Asp - metabolism Substrate recognition Substrate Specificity tRNA |
title | Ribonuclease P: a ribonucleoprotein enzyme |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T20%3A57%3A27IST&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=Ribonuclease%20P:%20a%20ribonucleoprotein%20enzyme&rft.jtitle=Current%20Opinion%20in%20Chemical%20Biology&rft.au=Kurz,%20Jeffrey%20C&rft.date=2000-10-01&rft.volume=4&rft.issue=5&rft.spage=553&rft.epage=558&rft.pages=553-558&rft.issn=1367-5931&rft.eissn=1879-0402&rft_id=info:doi/10.1016/S1367-5931(00)00131-9&rft_dat=%3Cproquest_cross%3E72304522%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=17638468&rft_id=info:pmid/11006544&rft_els_id=S1367593100001319&rfr_iscdi=true |