RNase PH: An Escherichia coli Phosphate-Dependent Nuclease Distinct from Polynucleotide Phosphorylase
Final trimming of the 3′ terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA normally. Extracts from such a multiple-RNase-defi...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1988-07, Vol.85 (13), p.4710-4714 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Deutscher, Murray P. Marshall, G. Thomas Cudny, Henryk |
| description | Final trimming of the 3′ terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA normally. Extracts from such a multiple-RNase-deficient strain accurately mature tRNA precursors exonucleolytically in vitro in a reaction that requires inorganic phosphate. Here we show that this reaction is not due to polynucleotide phosphorylase (PNPase) but, rather, that it is mediated by a phosphate-requiring exonuclease that we have named RNase PH. Purified PNPase is incapable of completely processing tRNA precursors, and extracts from a PNPase- strain retain full activity for phosphorolytic processing. Although both PNPase and RNase PH act in a phosphorolytic manner, they differ substantially in size and substrate specificity. RNase PH has a molecular mass of 45-50 kDa and favors tRNA precursors as substrates. The possible physiological role of RNase PH and the advantages of phosphorolytic processing are discussed. |
| doi_str_mv | 10.1073/pnas.85.13.4710 |
| format | Article |
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Thomas ; Cudny, Henryk</creator><creatorcontrib>Deutscher, Murray P. ; Marshall, G. Thomas ; Cudny, Henryk</creatorcontrib><description>Final trimming of the 3′ terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA normally. Extracts from such a multiple-RNase-deficient strain accurately mature tRNA precursors exonucleolytically in vitro in a reaction that requires inorganic phosphate. Here we show that this reaction is not due to polynucleotide phosphorylase (PNPase) but, rather, that it is mediated by a phosphate-requiring exonuclease that we have named RNase PH. Purified PNPase is incapable of completely processing tRNA precursors, and extracts from a PNPase- strain retain full activity for phosphorolytic processing. Although both PNPase and RNase PH act in a phosphorolytic manner, they differ substantially in size and substrate specificity. RNase PH has a molecular mass of 45-50 kDa and favors tRNA precursors as substrates. The possible physiological role of RNase PH and the advantages of phosphorolytic processing are discussed.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.85.13.4710</identifier><identifier>PMID: 2455297</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biological and medical sciences ; Chromatography, Gel ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Exoribonucleases - isolation & purification ; Exoribonucleases - metabolism ; Fundamental and applied biological sciences. Psychology ; Gels ; Gene expression ; Molecular and cellular biology ; Molecular genetics ; Molecular Weight ; Nucleotides ; Phosphates - metabolism ; Polynucleotides ; Polyribonucleotide Nucleotidyltransferase - metabolism ; Radioactive decay ; RNA ; RNA precursors ; RNA Precursors - metabolism ; RNA Processing, Post-Transcriptional ; RNA, Bacterial - metabolism ; Substrate specificity ; Transfer RNA</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1988-07, Vol.85 (13), p.4710-4714</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c587t-67d9280c02567dae02d50f3b678d9536e3816a2dba7e2d4fff5d3ff5f7a467a93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/85/13.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/31857$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/31857$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7145157$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2455297$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Deutscher, Murray P.</creatorcontrib><creatorcontrib>Marshall, G. Thomas</creatorcontrib><creatorcontrib>Cudny, Henryk</creatorcontrib><title>RNase PH: An Escherichia coli Phosphate-Dependent Nuclease Distinct from Polynucleotide Phosphorylase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Final trimming of the 3′ terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA normally. Extracts from such a multiple-RNase-deficient strain accurately mature tRNA precursors exonucleolytically in vitro in a reaction that requires inorganic phosphate. Here we show that this reaction is not due to polynucleotide phosphorylase (PNPase) but, rather, that it is mediated by a phosphate-requiring exonuclease that we have named RNase PH. Purified PNPase is incapable of completely processing tRNA precursors, and extracts from a PNPase- strain retain full activity for phosphorolytic processing. Although both PNPase and RNase PH act in a phosphorolytic manner, they differ substantially in size and substrate specificity. RNase PH has a molecular mass of 45-50 kDa and favors tRNA precursors as substrates. The possible physiological role of RNase PH and the advantages of phosphorolytic processing are discussed.</description><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Exoribonucleases - isolation & purification</subject><subject>Exoribonucleases - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Gene expression</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Weight</subject><subject>Nucleotides</subject><subject>Phosphates - metabolism</subject><subject>Polynucleotides</subject><subject>Polyribonucleotide Nucleotidyltransferase - metabolism</subject><subject>Radioactive decay</subject><subject>RNA</subject><subject>RNA precursors</subject><subject>RNA Precursors - metabolism</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>RNA, Bacterial - metabolism</subject><subject>Substrate specificity</subject><subject>Transfer RNA</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEcxYModa2eBUGZg-hptvkxmSSCh9JWK5S6iJ5DNpM4KdnJmGTE_e_NsONiL3pJAu_zvu8bHgDPEVwjyMjZOKi05nSNyLphCD4AKwQFqttGwIdgBSFmNW9w8xg8SekOQigohyfgBDeUYsFWwHy5VclUm-t31flQXSXdm-h071Slg3fVpg9p7FU29aUZzdCZIVe3k_ZmNl26lN2gc2Vj2FWb4PfDLIXsOrM4Q9z7gj4Fj6zyyTxb7lPw7cPV14vr-ubzx08X5ze1ppzlumWdwBxqiGl5KgNxR6El25bxTlDSGsJRq3C3VczgrrHW0o6UwzLVtEwJcgreH-aO03ZnOl3WjcrLMbqdinsZlJP3lcH18nv4KUsqhbT43yz-GH5MJmW5c0kb79VgwpQk41gITsR_QUQhakQDC3h2AHUMKUVjj8sgKOcG5dyg5FQiIucGi-Pl33848ktlRX-96Cpp5W1Ug3bpiDHUUERn7NWCzfP_qPdy3v4TkHbyPptfuZAvDuRdyiEeUYJ4yfkNEjrHAw</recordid><startdate>19880701</startdate><enddate>19880701</enddate><creator>Deutscher, Murray P.</creator><creator>Marshall, G. Thomas</creator><creator>Cudny, Henryk</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19880701</creationdate><title>RNase PH: An Escherichia coli Phosphate-Dependent Nuclease Distinct from Polynucleotide Phosphorylase</title><author>Deutscher, Murray P. ; Marshall, G. Thomas ; Cudny, Henryk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c587t-67d9280c02567dae02d50f3b678d9536e3816a2dba7e2d4fff5d3ff5f7a467a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Exoribonucleases - isolation & purification</topic><topic>Exoribonucleases - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Gene expression</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Weight</topic><topic>Nucleotides</topic><topic>Phosphates - metabolism</topic><topic>Polynucleotides</topic><topic>Polyribonucleotide Nucleotidyltransferase - metabolism</topic><topic>Radioactive decay</topic><topic>RNA</topic><topic>RNA precursors</topic><topic>RNA Precursors - metabolism</topic><topic>RNA Processing, Post-Transcriptional</topic><topic>RNA, Bacterial - metabolism</topic><topic>Substrate specificity</topic><topic>Transfer RNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Deutscher, Murray P.</creatorcontrib><creatorcontrib>Marshall, G. Thomas</creatorcontrib><creatorcontrib>Cudny, Henryk</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</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>Deutscher, Murray P.</au><au>Marshall, G. 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Here we show that this reaction is not due to polynucleotide phosphorylase (PNPase) but, rather, that it is mediated by a phosphate-requiring exonuclease that we have named RNase PH. Purified PNPase is incapable of completely processing tRNA precursors, and extracts from a PNPase- strain retain full activity for phosphorolytic processing. Although both PNPase and RNase PH act in a phosphorolytic manner, they differ substantially in size and substrate specificity. RNase PH has a molecular mass of 45-50 kDa and favors tRNA precursors as substrates. The possible physiological role of RNase PH and the advantages of phosphorolytic processing are discussed.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2455297</pmid><doi>10.1073/pnas.85.13.4710</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1988-07, Vol.85 (13), p.4710-4714 |
| issn | 0027-8424 1091-6490 |
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| subjects | Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biological and medical sciences Chromatography, Gel Enzymes Escherichia coli Escherichia coli - enzymology Exoribonucleases - isolation & purification Exoribonucleases - metabolism Fundamental and applied biological sciences. Psychology Gels Gene expression Molecular and cellular biology Molecular genetics Molecular Weight Nucleotides Phosphates - metabolism Polynucleotides Polyribonucleotide Nucleotidyltransferase - metabolism Radioactive decay RNA RNA precursors RNA Precursors - metabolism RNA Processing, Post-Transcriptional RNA, Bacterial - metabolism Substrate specificity Transfer RNA |
| title | RNase PH: An Escherichia coli Phosphate-Dependent Nuclease Distinct from Polynucleotide Phosphorylase |
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