Exoribonuclease superfamilies: structural analysis and phylogenetic distribution

Exoribonucleases play an important role in all aspects of RNA metabolism. Biochemical and genetic analyses in recent years have identified many new RNases and it is now clear that a single cell can contain multiple enzymes of this class. Here, we analyze the structure and phylogenetic distribution o...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nucleic acids research 2001-03, Vol.29 (5), p.1017-1026
Hauptverfasser: Zuo, Y, Deutscher, M P
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1026
container_issue 5
container_start_page 1017
container_title Nucleic acids research
container_volume 29
creator Zuo, Y
Deutscher, M P
description Exoribonucleases play an important role in all aspects of RNA metabolism. Biochemical and genetic analyses in recent years have identified many new RNases and it is now clear that a single cell can contain multiple enzymes of this class. Here, we analyze the structure and phylogenetic distribution of the known exoribonucleases. Based on extensive sequence analysis and on their catalytic properties, all of the exoribonucleases and their homologs have been grouped into six superfamilies and various subfamilies. We identify common motifs that can be used to characterize newly-discovered exoribonucleases, and based on these motifs we correct some previously misassigned proteins. This analysis may serve as a useful first step for developing a nomenclature for this group of enzymes.
doi_str_mv 10.1093/nar/29.5.1017
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_56904</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18215911</sourcerecordid><originalsourceid>FETCH-LOGICAL-c412t-41850c32f466bb89674c6575643d2e95dc7f6bea095372d6f5d12593e16bde613</originalsourceid><addsrcrecordid>eNqFkbtPwzAQxi0EgvIYWVEmthSfYzs1YkGoPKRKMMBsOc6lGKVxsWNE_3tSteIxMd13ut-dvtNHyCnQMVBVXHQmXDA1FkMH5Q4ZQSFZzpVku7_0ATmM8Y1S4CD4PjkAYIyVXI3I0_TTB1f5LtkWTcQspiWGxixc6zBeZrEPyfYpmDYznWlX0cVB1NnyddX6OXbYO5vVbsBclXrnu2Oy15g24sm2HpGX2-nzzX0-e7x7uLme5ZYD63MOE0FtwRouZVVNlCy5laIUkhc1QyVqWzayQkOVKEpWy0bUwIQqEGRVo4TiiFxt7i5TtcDaYtcPJvUyuIUJK-2N038nnXvVc_-hhVSUD-vn2_Xg3xPGXi9ctNi2pkOfoi6pHEBJ_wVhwkAoWBvKN6ANPsaAzbcXoHodlR6i0kxpoddRDfzZ7wd-6G02xRei_pI-</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18215911</pqid></control><display><type>article</type><title>Exoribonuclease superfamilies: structural analysis and phylogenetic distribution</title><source>MEDLINE</source><source>Oxford Journals Open Access Collection</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Zuo, Y ; Deutscher, M P</creator><creatorcontrib>Zuo, Y ; Deutscher, M P</creatorcontrib><description>Exoribonucleases play an important role in all aspects of RNA metabolism. Biochemical and genetic analyses in recent years have identified many new RNases and it is now clear that a single cell can contain multiple enzymes of this class. Here, we analyze the structure and phylogenetic distribution of the known exoribonucleases. Based on extensive sequence analysis and on their catalytic properties, all of the exoribonucleases and their homologs have been grouped into six superfamilies and various subfamilies. We identify common motifs that can be used to characterize newly-discovered exoribonucleases, and based on these motifs we correct some previously misassigned proteins. This analysis may serve as a useful first step for developing a nomenclature for this group of enzymes.</description><identifier>ISSN: 1362-4962</identifier><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/29.5.1017</identifier><identifier>PMID: 11222749</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Exoribonucleases - genetics ; Humans ; Molecular Sequence Data ; Phylogeny ; ribonuclease ; Sequence Alignment</subject><ispartof>Nucleic acids research, 2001-03, Vol.29 (5), p.1017-1026</ispartof><rights>Copyright © 2001 Oxford University Press 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-41850c32f466bb89674c6575643d2e95dc7f6bea095372d6f5d12593e16bde613</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/PMC56904/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC56904/$$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/11222749$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zuo, Y</creatorcontrib><creatorcontrib>Deutscher, M P</creatorcontrib><title>Exoribonuclease superfamilies: structural analysis and phylogenetic distribution</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Exoribonucleases play an important role in all aspects of RNA metabolism. Biochemical and genetic analyses in recent years have identified many new RNases and it is now clear that a single cell can contain multiple enzymes of this class. Here, we analyze the structure and phylogenetic distribution of the known exoribonucleases. Based on extensive sequence analysis and on their catalytic properties, all of the exoribonucleases and their homologs have been grouped into six superfamilies and various subfamilies. We identify common motifs that can be used to characterize newly-discovered exoribonucleases, and based on these motifs we correct some previously misassigned proteins. This analysis may serve as a useful first step for developing a nomenclature for this group of enzymes.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Exoribonucleases - genetics</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>ribonuclease</subject><subject>Sequence Alignment</subject><issn>1362-4962</issn><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkbtPwzAQxi0EgvIYWVEmthSfYzs1YkGoPKRKMMBsOc6lGKVxsWNE_3tSteIxMd13ut-dvtNHyCnQMVBVXHQmXDA1FkMH5Q4ZQSFZzpVku7_0ATmM8Y1S4CD4PjkAYIyVXI3I0_TTB1f5LtkWTcQspiWGxixc6zBeZrEPyfYpmDYznWlX0cVB1NnyddX6OXbYO5vVbsBclXrnu2Oy15g24sm2HpGX2-nzzX0-e7x7uLme5ZYD63MOE0FtwRouZVVNlCy5laIUkhc1QyVqWzayQkOVKEpWy0bUwIQqEGRVo4TiiFxt7i5TtcDaYtcPJvUyuIUJK-2N038nnXvVc_-hhVSUD-vn2_Xg3xPGXi9ctNi2pkOfoi6pHEBJ_wVhwkAoWBvKN6ANPsaAzbcXoHodlR6i0kxpoddRDfzZ7wd-6G02xRei_pI-</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>Zuo, Y</creator><creator>Deutscher, M P</creator><general>Oxford University Press</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><scope>5PM</scope></search><sort><creationdate>20010301</creationdate><title>Exoribonuclease superfamilies: structural analysis and phylogenetic distribution</title><author>Zuo, Y ; Deutscher, M P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-41850c32f466bb89674c6575643d2e95dc7f6bea095372d6f5d12593e16bde613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Exoribonucleases - genetics</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>ribonuclease</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zuo, Y</creatorcontrib><creatorcontrib>Deutscher, M P</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zuo, Y</au><au>Deutscher, M P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exoribonuclease superfamilies: structural analysis and phylogenetic distribution</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2001-03-01</date><risdate>2001</risdate><volume>29</volume><issue>5</issue><spage>1017</spage><epage>1026</epage><pages>1017-1026</pages><issn>1362-4962</issn><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Exoribonucleases play an important role in all aspects of RNA metabolism. Biochemical and genetic analyses in recent years have identified many new RNases and it is now clear that a single cell can contain multiple enzymes of this class. Here, we analyze the structure and phylogenetic distribution of the known exoribonucleases. Based on extensive sequence analysis and on their catalytic properties, all of the exoribonucleases and their homologs have been grouped into six superfamilies and various subfamilies. We identify common motifs that can be used to characterize newly-discovered exoribonucleases, and based on these motifs we correct some previously misassigned proteins. This analysis may serve as a useful first step for developing a nomenclature for this group of enzymes.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>11222749</pmid><doi>10.1093/nar/29.5.1017</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1362-4962
ispartof Nucleic acids research, 2001-03, Vol.29 (5), p.1017-1026
issn 1362-4962
0305-1048
1362-4962
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_56904
source MEDLINE; Oxford Journals Open Access Collection; PubMed Central; Free Full-Text Journals in Chemistry
subjects Amino Acid Sequence
Animals
Exoribonucleases - genetics
Humans
Molecular Sequence Data
Phylogeny
ribonuclease
Sequence Alignment
title Exoribonuclease superfamilies: structural analysis and phylogenetic distribution
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T18%3A54%3A32IST&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=Exoribonuclease%20superfamilies:%20structural%20analysis%20and%20phylogenetic%20distribution&rft.jtitle=Nucleic%20acids%20research&rft.au=Zuo,%20Y&rft.date=2001-03-01&rft.volume=29&rft.issue=5&rft.spage=1017&rft.epage=1026&rft.pages=1017-1026&rft.issn=1362-4962&rft.eissn=1362-4962&rft_id=info:doi/10.1093/nar/29.5.1017&rft_dat=%3Cproquest_pubme%3E18215911%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=18215911&rft_id=info:pmid/11222749&rfr_iscdi=true