Characterization of RNase P from Thermotoga maritima
The protein subunit of RNase P from a thermophilic bacterium, Thermotoga maritima, was overexpressed in and purified from Escherichia coli. The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50 degrees C, with no enzymati...
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| Veröffentlicht in: | Nucleic acids research 2001-02, Vol.29 (4), p.880-885 |
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| creator | Paul, R Lazarev, D Altman, S |
| description | The protein subunit of RNase P from a thermophilic bacterium, Thermotoga maritima, was overexpressed in and purified from Escherichia coli. The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50 degrees C, with no enzymatic activity at 65 degrees C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80 degrees C. However, in heterologous reconstitution experiments in vitro with RNase P subunits from other species, we found that the protein subunit from T.maritima was responsible for the comparative thermal stability of such complexes. |
| doi_str_mv | 10.1093/nar/29.4.880 |
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The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50 degrees C, with no enzymatic activity at 65 degrees C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80 degrees C. However, in heterologous reconstitution experiments in vitro with RNase P subunits from other species, we found that the protein subunit from T.maritima was responsible for the comparative thermal stability of such complexes.</description><identifier>ISSN: 1362-4962</identifier><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/29.4.880</identifier><identifier>PMID: 11160919</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford Publishing Limited (England)</publisher><subject>Amino Acid Sequence ; Amino Acids - analysis ; Endoribonucleases - chemistry ; Endoribonucleases - genetics ; Endoribonucleases - isolation & purification ; Endoribonucleases - metabolism ; Enzyme Stability ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli Proteins ; Holoenzymes - chemistry ; Holoenzymes - genetics ; Holoenzymes - isolation & purification ; Holoenzymes - metabolism ; Kinetics ; Molecular Sequence Data ; Protein Subunits ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - metabolism ; Ribonuclease P ; RNA, Bacterial - genetics ; RNA, Bacterial - isolation & purification ; RNA, Bacterial - metabolism ; RNA, Catalytic - chemistry ; RNA, Catalytic - genetics ; RNA, Catalytic - isolation & purification ; RNA, Catalytic - metabolism ; RNA, Transfer, Tyr - genetics ; RNA, Transfer, Tyr - metabolism ; Sequence Alignment ; Temperature ; Thermotoga maritima ; Thermotoga maritima - enzymology ; Thermotoga maritima - genetics ; Transcription, Genetic</subject><ispartof>Nucleic acids research, 2001-02, Vol.29 (4), p.880-885</ispartof><rights>Copyright Oxford University Press(England) Feb 15, 2001</rights><rights>Copyright © 2001 Oxford University Press 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c436t-c8e7df7ef9f80d225054197235d9cccc8c89f605122d118f9d008e7a1eb3a3993</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/PMC29617/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC29617/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,27928,27929,53795,53797</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11160919$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Paul, R</creatorcontrib><creatorcontrib>Lazarev, D</creatorcontrib><creatorcontrib>Altman, S</creatorcontrib><title>Characterization of RNase P from Thermotoga maritima</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>The protein subunit of RNase P from a thermophilic bacterium, Thermotoga maritima, was overexpressed in and purified from Escherichia coli. The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50 degrees C, with no enzymatic activity at 65 degrees C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80 degrees C. However, in heterologous reconstitution experiments in vitro with RNase P subunits from other species, we found that the protein subunit from T.maritima was responsible for the comparative thermal stability of such complexes.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Endoribonucleases - chemistry</subject><subject>Endoribonucleases - genetics</subject><subject>Endoribonucleases - isolation & purification</subject><subject>Endoribonucleases - metabolism</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins</subject><subject>Holoenzymes - chemistry</subject><subject>Holoenzymes - genetics</subject><subject>Holoenzymes - isolation & purification</subject><subject>Holoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Protein Subunits</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Ribonuclease P</subject><subject>RNA, Bacterial - genetics</subject><subject>RNA, Bacterial - isolation & purification</subject><subject>RNA, Bacterial - metabolism</subject><subject>RNA, Catalytic - chemistry</subject><subject>RNA, Catalytic - genetics</subject><subject>RNA, Catalytic - isolation & purification</subject><subject>RNA, Catalytic - metabolism</subject><subject>RNA, Transfer, Tyr - genetics</subject><subject>RNA, Transfer, Tyr - metabolism</subject><subject>Sequence Alignment</subject><subject>Temperature</subject><subject>Thermotoga maritima</subject><subject>Thermotoga maritima - enzymology</subject><subject>Thermotoga maritima - genetics</subject><subject>Transcription, Genetic</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>eNqFkc9LwzAcxYMoTqc3z1I8eLJbvkmaNOBFhr9gqMg8h6xNto61mUkr6F9vZEOnF7-XfCGfF17eQ-gE8ACwpMNG-yGRAzbIc7yDDoBykjLJye7W3kOHISwwBgYZ20c9AOBYgjxAbDTXXhet8dWHbivXJM4mzw86mOQpsd7VyWRufO1aN9NJrX3VVrU-QntWL4M53px99HJzPRndpePH2_vR1TgtGOVtWuRGlFYYK22OS0IynDGQgtCslEWcvMil5TgDQkqA3MoS4yjRYKZUUylpH12u311109qUhWlar5dq5aMH_66crtTvm6aaq5l7U0RyEFF-vpF799qZ0Kq6CoVZLnVjXBeUwJxxwbN_Qchj0CIa76OzP-DCdb6JGSiCccYFxRChizVUeBeCN_bbMGD1VZmKlUWLiqlYWcRPtz_5A286op9UJZGR</recordid><startdate>20010215</startdate><enddate>20010215</enddate><creator>Paul, R</creator><creator>Lazarev, D</creator><creator>Altman, S</creator><general>Oxford Publishing Limited (England)</general><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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010215</creationdate><title>Characterization of RNase P from Thermotoga maritima</title><author>Paul, R ; Lazarev, D ; Altman, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-c8e7df7ef9f80d225054197235d9cccc8c89f605122d118f9d008e7a1eb3a3993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Endoribonucleases - chemistry</topic><topic>Endoribonucleases - genetics</topic><topic>Endoribonucleases - isolation & purification</topic><topic>Endoribonucleases - metabolism</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins</topic><topic>Holoenzymes - chemistry</topic><topic>Holoenzymes - genetics</topic><topic>Holoenzymes - isolation & purification</topic><topic>Holoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Protein Subunits</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Ribonuclease P</topic><topic>RNA, Bacterial - genetics</topic><topic>RNA, Bacterial - isolation & purification</topic><topic>RNA, Bacterial - metabolism</topic><topic>RNA, Catalytic - chemistry</topic><topic>RNA, Catalytic - genetics</topic><topic>RNA, Catalytic - isolation & purification</topic><topic>RNA, Catalytic - metabolism</topic><topic>RNA, Transfer, Tyr - genetics</topic><topic>RNA, Transfer, Tyr - metabolism</topic><topic>Sequence Alignment</topic><topic>Temperature</topic><topic>Thermotoga maritima</topic><topic>Thermotoga maritima - enzymology</topic><topic>Thermotoga maritima - genetics</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Paul, R</creatorcontrib><creatorcontrib>Lazarev, D</creatorcontrib><creatorcontrib>Altman, S</creatorcontrib><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>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>ProQuest Health & Medical Complete (Alumni)</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>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Paul, R</au><au>Lazarev, D</au><au>Altman, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of RNase P from Thermotoga maritima</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2001-02-15</date><risdate>2001</risdate><volume>29</volume><issue>4</issue><spage>880</spage><epage>885</epage><pages>880-885</pages><issn>1362-4962</issn><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>The protein subunit of RNase P from a thermophilic bacterium, Thermotoga maritima, was overexpressed in and purified from Escherichia coli. The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50 degrees C, with no enzymatic activity at 65 degrees C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80 degrees C. However, in heterologous reconstitution experiments in vitro with RNase P subunits from other species, we found that the protein subunit from T.maritima was responsible for the comparative thermal stability of such complexes.</abstract><cop>England</cop><pub>Oxford Publishing Limited (England)</pub><pmid>11160919</pmid><doi>10.1093/nar/29.4.880</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acids - analysis Endoribonucleases - chemistry Endoribonucleases - genetics Endoribonucleases - isolation & purification Endoribonucleases - metabolism Enzyme Stability Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins Holoenzymes - chemistry Holoenzymes - genetics Holoenzymes - isolation & purification Holoenzymes - metabolism Kinetics Molecular Sequence Data Protein Subunits Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Ribonuclease P RNA, Bacterial - genetics RNA, Bacterial - isolation & purification RNA, Bacterial - metabolism RNA, Catalytic - chemistry RNA, Catalytic - genetics RNA, Catalytic - isolation & purification RNA, Catalytic - metabolism RNA, Transfer, Tyr - genetics RNA, Transfer, Tyr - metabolism Sequence Alignment Temperature Thermotoga maritima Thermotoga maritima - enzymology Thermotoga maritima - genetics Transcription, Genetic |
| title | Characterization of RNase P from Thermotoga maritima |
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