Partial characterization of the ribonuclease P from Tetrahymena pyriformis
Ribonuclease P activity from infusoria Tetrahymena pyriformis has been isolated and purified more than 1000-fold over cytosol crude extract. Purified tRNA 5′ endonuclease processes in vitro heterologous, substrates, precursors of the human tRNA Tyr and Drosophila melanogaster tRNA Len, exactly at th...
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Veröffentlicht in: | Biochimie 1998-07, Vol.80 (7), p.595-604 |
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creator | Vainauskas, Saulius Stribinskis, Vilius Padegimas, Linas Juodka, Benediktas |
description | Ribonuclease P activity from infusoria
Tetrahymena pyriformis has been isolated and purified more than 1000-fold over cytosol crude extract. Purified tRNA 5′ endonuclease processes in vitro heterologous, substrates, precursors of the human tRNA
Tyr and
Drosophila melanogaster tRNA
Len, exactly at the 5′ end of the mature molecules. The activity was abolished by micrococcal nuclease and protease treatment indicating that both RNA and protein components are essential for its activity. The most abundant polypeptides in the purified enzyme fractions have molecular masses of about 100, 44 and 35 kDa. The enzyme requires divalent cations for its activity and shows optimal activity in the presence of the low concentrations of the monovalent salts. Substrate structural requirements for the purified enzyme were analyzed with different tRNA precursor models. The analysis of the derivatives of tRNA
Leu precursors with altered aminoacyl stem structures reveals that end of the stem is important for substrate 5′ end processing with purified enzyme. |
doi_str_mv | 10.1016/S0300-9084(98)80012-6 |
format | Article |
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Tetrahymena pyriformis has been isolated and purified more than 1000-fold over cytosol crude extract. Purified tRNA 5′ endonuclease processes in vitro heterologous, substrates, precursors of the human tRNA
Tyr and
Drosophila melanogaster tRNA
Len, exactly at the 5′ end of the mature molecules. The activity was abolished by micrococcal nuclease and protease treatment indicating that both RNA and protein components are essential for its activity. The most abundant polypeptides in the purified enzyme fractions have molecular masses of about 100, 44 and 35 kDa. The enzyme requires divalent cations for its activity and shows optimal activity in the presence of the low concentrations of the monovalent salts. Substrate structural requirements for the purified enzyme were analyzed with different tRNA precursor models. The analysis of the derivatives of tRNA
Leu precursors with altered aminoacyl stem structures reveals that end of the stem is important for substrate 5′ end processing with purified enzyme.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/S0300-9084(98)80012-6</identifier><identifier>PMID: 9810466</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Animals ; Base Sequence ; Drosophila melanogaster ; Endoribonucleases - chemistry ; Endoribonucleases - isolation & purification ; Humans ; Molecular Sequence Data ; Nucleic Acid Conformation ; Ribonuclease P ; RNA Precursors - chemistry ; RNA, Catalytic - chemistry ; RNA, Catalytic - isolation & purification ; RNA, Transfer, Leu - chemistry ; RNA, Transfer, Tyr - chemistry ; Substrate Specificity ; Tetrahymena pyriformis ; Tetrahymena pyriformis - enzymology ; tRNA</subject><ispartof>Biochimie, 1998-07, Vol.80 (7), p.595-604</ispartof><rights>1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-6043567fff6c1988cf009170e1b1e79b8d16642be81f93a0c5c94d192723d8453</citedby><cites>FETCH-LOGICAL-c360t-6043567fff6c1988cf009170e1b1e79b8d16642be81f93a0c5c94d192723d8453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0300-9084(98)80012-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9810466$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vainauskas, Saulius</creatorcontrib><creatorcontrib>Stribinskis, Vilius</creatorcontrib><creatorcontrib>Padegimas, Linas</creatorcontrib><creatorcontrib>Juodka, Benediktas</creatorcontrib><title>Partial characterization of the ribonuclease P from Tetrahymena pyriformis</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Ribonuclease P activity from infusoria
Tetrahymena pyriformis has been isolated and purified more than 1000-fold over cytosol crude extract. Purified tRNA 5′ endonuclease processes in vitro heterologous, substrates, precursors of the human tRNA
Tyr and
Drosophila melanogaster tRNA
Len, exactly at the 5′ end of the mature molecules. The activity was abolished by micrococcal nuclease and protease treatment indicating that both RNA and protein components are essential for its activity. The most abundant polypeptides in the purified enzyme fractions have molecular masses of about 100, 44 and 35 kDa. The enzyme requires divalent cations for its activity and shows optimal activity in the presence of the low concentrations of the monovalent salts. Substrate structural requirements for the purified enzyme were analyzed with different tRNA precursor models. The analysis of the derivatives of tRNA
Leu precursors with altered aminoacyl stem structures reveals that end of the stem is important for substrate 5′ end processing with purified enzyme.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Drosophila melanogaster</subject><subject>Endoribonucleases - chemistry</subject><subject>Endoribonucleases - isolation & purification</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Ribonuclease P</subject><subject>RNA Precursors - chemistry</subject><subject>RNA, Catalytic - chemistry</subject><subject>RNA, Catalytic - isolation & purification</subject><subject>RNA, Transfer, Leu - chemistry</subject><subject>RNA, Transfer, Tyr - chemistry</subject><subject>Substrate Specificity</subject><subject>Tetrahymena pyriformis</subject><subject>Tetrahymena pyriformis - enzymology</subject><subject>tRNA</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFtLwzAUx4Moc04_wqBPog_Vk17S5ElkeGXgwPkc0vSERdpmJq0wP73dBV99Og__G-dHyJTCDQXKbt8hBYgF8OxK8GsOQJOYHZExZSmPGeXpMRn_WU7JWQifAJBDIkZkJDiFjLExeV0o31lVR3qlvNIdevujOuvayJmoW2HkbenaXteoAkaLyHjXREvsvFptGmxVtN54a5xvbDgnJ0bVAS8Od0I-Hh-Ws-d4_vb0Mrufxzpl0MUMsjRnhTGGaSo41wZA0AKQlhQLUfKKMpYlJXJqRKpA51pkFRVJkaQVz_J0Qi73vWvvvnoMnRzGNda1atH1QRYAWVYkfDDme6P2LgSPRq69bZTfSApyy1DuGMotICm43DGUbMhNDwN92WD1lzpAG_S7vY7Dl98WvQzaYquxsh51Jytn_1n4BRrUgHs</recordid><startdate>19980701</startdate><enddate>19980701</enddate><creator>Vainauskas, Saulius</creator><creator>Stribinskis, Vilius</creator><creator>Padegimas, Linas</creator><creator>Juodka, Benediktas</creator><general>Elsevier Masson SAS</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>7X8</scope></search><sort><creationdate>19980701</creationdate><title>Partial characterization of the ribonuclease P from Tetrahymena pyriformis</title><author>Vainauskas, Saulius ; Stribinskis, Vilius ; Padegimas, Linas ; Juodka, Benediktas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-6043567fff6c1988cf009170e1b1e79b8d16642be81f93a0c5c94d192723d8453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Drosophila melanogaster</topic><topic>Endoribonucleases - chemistry</topic><topic>Endoribonucleases - isolation & purification</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Ribonuclease P</topic><topic>RNA Precursors - chemistry</topic><topic>RNA, Catalytic - chemistry</topic><topic>RNA, Catalytic - isolation & purification</topic><topic>RNA, Transfer, Leu - chemistry</topic><topic>RNA, Transfer, Tyr - chemistry</topic><topic>Substrate Specificity</topic><topic>Tetrahymena pyriformis</topic><topic>Tetrahymena pyriformis - enzymology</topic><topic>tRNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vainauskas, Saulius</creatorcontrib><creatorcontrib>Stribinskis, Vilius</creatorcontrib><creatorcontrib>Padegimas, Linas</creatorcontrib><creatorcontrib>Juodka, Benediktas</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vainauskas, Saulius</au><au>Stribinskis, Vilius</au><au>Padegimas, Linas</au><au>Juodka, Benediktas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Partial characterization of the ribonuclease P from Tetrahymena pyriformis</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>1998-07-01</date><risdate>1998</risdate><volume>80</volume><issue>7</issue><spage>595</spage><epage>604</epage><pages>595-604</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Ribonuclease P activity from infusoria
Tetrahymena pyriformis has been isolated and purified more than 1000-fold over cytosol crude extract. Purified tRNA 5′ endonuclease processes in vitro heterologous, substrates, precursors of the human tRNA
Tyr and
Drosophila melanogaster tRNA
Len, exactly at the 5′ end of the mature molecules. The activity was abolished by micrococcal nuclease and protease treatment indicating that both RNA and protein components are essential for its activity. The most abundant polypeptides in the purified enzyme fractions have molecular masses of about 100, 44 and 35 kDa. The enzyme requires divalent cations for its activity and shows optimal activity in the presence of the low concentrations of the monovalent salts. Substrate structural requirements for the purified enzyme were analyzed with different tRNA precursor models. The analysis of the derivatives of tRNA
Leu precursors with altered aminoacyl stem structures reveals that end of the stem is important for substrate 5′ end processing with purified enzyme.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>9810466</pmid><doi>10.1016/S0300-9084(98)80012-6</doi><tpages>10</tpages></addata></record> |
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subjects | Animals Base Sequence Drosophila melanogaster Endoribonucleases - chemistry Endoribonucleases - isolation & purification Humans Molecular Sequence Data Nucleic Acid Conformation Ribonuclease P RNA Precursors - chemistry RNA, Catalytic - chemistry RNA, Catalytic - isolation & purification RNA, Transfer, Leu - chemistry RNA, Transfer, Tyr - chemistry Substrate Specificity Tetrahymena pyriformis Tetrahymena pyriformis - enzymology tRNA |
title | Partial characterization of the ribonuclease P from Tetrahymena pyriformis |
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