RNase P Cleaves Transient Structures in Some Riboswitches
RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-08, Vol.102 (32), p.11284-11289 |
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| creator | Altman, Sidney Wesolowski, Donna Guerrier-Takada, Cecilia Li, Yong |
| description | RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme that is a good representation of the E. coli cleavage site for RNase P and for the cleavage site in B. subtilis. These data indicate that transient structures are important in RNase P cleavage and in riboswitch function. Coenzyme B12 has a small inhibitory effect on E. coli RNase P cleavage of the E. coli riboswitch. Both E. coli RNase P and a partially purified RNase P from Aspergillus nidulans mycelia succeeded in cleaving a putative arginine riboswitch from A. nidulans. The cleavage site may be a representative of another model substrate for eukaryotic RNase P. This 5′ UTR controls splicing of the arginase mRNA in A. nidulans. Four other riboswitches in E. coli were not cleaved by RNase P under the conditions tested. |
| doi_str_mv | 10.1073/pnas.0505271102 |
| format | Article |
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The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme that is a good representation of the E. coli cleavage site for RNase P and for the cleavage site in B. subtilis. These data indicate that transient structures are important in RNase P cleavage and in riboswitch function. Coenzyme B12 has a small inhibitory effect on E. coli RNase P cleavage of the E. coli riboswitch. Both E. coli RNase P and a partially purified RNase P from Aspergillus nidulans mycelia succeeded in cleaving a putative arginine riboswitch from A. nidulans. The cleavage site may be a representative of another model substrate for eukaryotic RNase P. This 5′ UTR controls splicing of the arginase mRNA in A. nidulans. Four other riboswitches in E. coli were not cleaved by RNase P under the conditions tested.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0505271102</identifier><identifier>PMID: 16061811</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Aspergillus nidulans ; Bacillus subtilis ; Bacterial proteins ; Base Pairing ; Base Sequence ; beta-Galactosidase ; Biological Sciences ; Cloning, Molecular ; Cobamides - genetics ; Cobamides - metabolism ; Coenzymes ; DNA Primers ; Enzymes ; Escherichia coli ; Gene Expression Regulation ; Genes ; Messenger RNA ; Molecular Sequence Data ; Mutation - genetics ; Nucleotides ; Open reading frames ; Operator regions ; Plasmids - genetics ; Regulatory Sequences, Nucleic Acid - genetics ; Ribonuclease P - metabolism ; Ribozymes ; RNA ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Transfer RNA ; Untranslated regions</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-08, Vol.102 (32), p.11284-11289</ispartof><rights>Copyright 1993/2005 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Aug 9, 2005</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c529t-150c6c468cf6fe00783f960a2377f4d056f5fb9beecb646b6d209252d0a999a3</citedby><cites>FETCH-LOGICAL-c529t-150c6c468cf6fe00783f960a2377f4d056f5fb9beecb646b6d209252d0a999a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/32.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3376259$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3376259$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16061811$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Altman, Sidney</creatorcontrib><creatorcontrib>Wesolowski, Donna</creatorcontrib><creatorcontrib>Guerrier-Takada, Cecilia</creatorcontrib><creatorcontrib>Li, Yong</creatorcontrib><title>RNase P Cleaves Transient Structures in Some Riboswitches</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme that is a good representation of the E. coli cleavage site for RNase P and for the cleavage site in B. subtilis. These data indicate that transient structures are important in RNase P cleavage and in riboswitch function. Coenzyme B12 has a small inhibitory effect on E. coli RNase P cleavage of the E. coli riboswitch. Both E. coli RNase P and a partially purified RNase P from Aspergillus nidulans mycelia succeeded in cleaving a putative arginine riboswitch from A. nidulans. The cleavage site may be a representative of another model substrate for eukaryotic RNase P. This 5′ UTR controls splicing of the arginase mRNA in A. nidulans. Four other riboswitches in E. coli were not cleaved by RNase P under the conditions tested.</description><subject>Aspergillus nidulans</subject><subject>Bacillus subtilis</subject><subject>Bacterial proteins</subject><subject>Base Pairing</subject><subject>Base Sequence</subject><subject>beta-Galactosidase</subject><subject>Biological Sciences</subject><subject>Cloning, Molecular</subject><subject>Cobamides - genetics</subject><subject>Cobamides - metabolism</subject><subject>Coenzymes</subject><subject>DNA Primers</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Gene Expression Regulation</subject><subject>Genes</subject><subject>Messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Nucleotides</subject><subject>Open reading frames</subject><subject>Operator regions</subject><subject>Plasmids - genetics</subject><subject>Regulatory Sequences, Nucleic Acid - genetics</subject><subject>Ribonuclease P - metabolism</subject><subject>Ribozymes</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Transfer RNA</subject><subject>Untranslated regions</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9LHDEUB_BQKnW1PfdSyuBB8DD6kkx-XQplsbUgWnTvIZNN6iyzk22S8cd_b5Zd3NaLp0DyeY-890XoM4ZTDIKerQaTToEBIwJjIO_QBIPCNW8UvEcTACJq2ZBmHx2ktAAAxSR8QPuYA8cS4wlSN1cmuep3Ne2duXepmkUzpM4NubrNcbR5jOWyG6rbsHTVTdeG9NBle-fSR7TnTZ_cp-15iGY_zmfTi_ry-uev6ffL2jKico0ZWG4bLq3n3gEISb3iYAgVwjdzYNwz36rWOdvyhrd8TkARRuZglFKGHqJvm7arsV26uS0_i6bXq9gtTXzSwXT6_5ehu9N_wr3GWFIOuDQ43jaI4e_oUtbLLlnX92ZwYUyay4YroM2bkJSFMyZVgUev4CKMcShLKAZTQQVmBZ1tkI0hpej8y5cx6HV2ep2d3mVXKr7-O-nOb8MqoNqCdeWuHdGUlHGJXM9w8gbRfuz77B5zsV82dpFyiC-YUsEJU_QZC4u2IQ</recordid><startdate>20050809</startdate><enddate>20050809</enddate><creator>Altman, Sidney</creator><creator>Wesolowski, Donna</creator><creator>Guerrier-Takada, Cecilia</creator><creator>Li, Yong</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050809</creationdate><title>RNase P Cleaves Transient Structures in Some Riboswitches</title><author>Altman, Sidney ; Wesolowski, Donna ; Guerrier-Takada, Cecilia ; Li, Yong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c529t-150c6c468cf6fe00783f960a2377f4d056f5fb9beecb646b6d209252d0a999a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Aspergillus nidulans</topic><topic>Bacillus subtilis</topic><topic>Bacterial proteins</topic><topic>Base Pairing</topic><topic>Base Sequence</topic><topic>beta-Galactosidase</topic><topic>Biological Sciences</topic><topic>Cloning, Molecular</topic><topic>Cobamides - genetics</topic><topic>Cobamides - metabolism</topic><topic>Coenzymes</topic><topic>DNA Primers</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Gene Expression Regulation</topic><topic>Genes</topic><topic>Messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>Nucleotides</topic><topic>Open reading frames</topic><topic>Operator regions</topic><topic>Plasmids - genetics</topic><topic>Regulatory Sequences, Nucleic Acid - genetics</topic><topic>Ribonuclease P - metabolism</topic><topic>Ribozymes</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Transfer RNA</topic><topic>Untranslated regions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Altman, Sidney</creatorcontrib><creatorcontrib>Wesolowski, Donna</creatorcontrib><creatorcontrib>Guerrier-Takada, Cecilia</creatorcontrib><creatorcontrib>Li, Yong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Altman, Sidney</au><au>Wesolowski, Donna</au><au>Guerrier-Takada, Cecilia</au><au>Li, Yong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RNase P Cleaves Transient Structures in Some Riboswitches</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-08-09</date><risdate>2005</risdate><volume>102</volume><issue>32</issue><spage>11284</spage><epage>11289</epage><pages>11284-11289</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme that is a good representation of the E. coli cleavage site for RNase P and for the cleavage site in B. subtilis. These data indicate that transient structures are important in RNase P cleavage and in riboswitch function. Coenzyme B12 has a small inhibitory effect on E. coli RNase P cleavage of the E. coli riboswitch. Both E. coli RNase P and a partially purified RNase P from Aspergillus nidulans mycelia succeeded in cleaving a putative arginine riboswitch from A. nidulans. The cleavage site may be a representative of another model substrate for eukaryotic RNase P. This 5′ UTR controls splicing of the arginase mRNA in A. nidulans. Four other riboswitches in E. coli were not cleaved by RNase P under the conditions tested.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16061811</pmid><doi>10.1073/pnas.0505271102</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Aspergillus nidulans Bacillus subtilis Bacterial proteins Base Pairing Base Sequence beta-Galactosidase Biological Sciences Cloning, Molecular Cobamides - genetics Cobamides - metabolism Coenzymes DNA Primers Enzymes Escherichia coli Gene Expression Regulation Genes Messenger RNA Molecular Sequence Data Mutation - genetics Nucleotides Open reading frames Operator regions Plasmids - genetics Regulatory Sequences, Nucleic Acid - genetics Ribonuclease P - metabolism Ribozymes RNA RNA, Messenger - genetics RNA, Messenger - metabolism Transfer RNA Untranslated regions |
| title | RNase P Cleaves Transient Structures in Some Riboswitches |
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