Primer-independent abortive initiation by wheat-germ RNA polymerase B (II)
Highly purified RNA polymerase B (II) from wheat germ catalyses the formation of dinucleoside tetraphosphates from ribonucleoside triphosphates in the absence of an oligonucleotide primer or additional protein factors. The reaction requires bivalent cations such as Mn2+ or Mg2+ and proceeds linearly...
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Veröffentlicht in: | European journal of biochemistry 1985-01, Vol.149 (2), p.337-343 |
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creator | Mosig, H Schaffner, A.R Sieber, H Hartmann, G.R |
description | Highly purified RNA polymerase B (II) from wheat germ catalyses the formation of dinucleoside tetraphosphates from ribonucleoside triphosphates in the absence of an oligonucleotide primer or additional protein factors. The reaction requires bivalent cations such as Mn2+ or Mg2+ and proceeds linearly for several hours. It is strongly inhibited by 1 μg/ml α‐amanitin or 2 μg/ml heparin. The reaction strictly depends on the addition of a specific linear or circular DNA template, such as the plasmid pSmaF or a DNA fragment containing the gene for nopaline dehydrogenase. Bacteriophage T7 D111 DNA has almost no template activity. The start sites for dinucleotide synthesis on the template are limited. With the DNA fragment containing the gene for nopaline dehydrogenase only pppApA and pppApU are synthesised substantially whereas pppUpU is formed only in trace amounts. No significant dinucleotide synthesis is observed with other ribonucleoside triphosphates either singly or in a combination of two. The various regions of the DNA fragment differ distinctly in template activity. |
doi_str_mv | 10.1111/j.1432-1033.1985.tb08931.x |
format | Article |
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The reaction requires bivalent cations such as Mn2+ or Mg2+ and proceeds linearly for several hours. It is strongly inhibited by 1 μg/ml α‐amanitin or 2 μg/ml heparin. The reaction strictly depends on the addition of a specific linear or circular DNA template, such as the plasmid pSmaF or a DNA fragment containing the gene for nopaline dehydrogenase. Bacteriophage T7 D111 DNA has almost no template activity. The start sites for dinucleotide synthesis on the template are limited. With the DNA fragment containing the gene for nopaline dehydrogenase only pppApA and pppApU are synthesised substantially whereas pppUpU is formed only in trace amounts. No significant dinucleotide synthesis is observed with other ribonucleoside triphosphates either singly or in a combination of two. The various regions of the DNA fragment differ distinctly in template activity.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1985.tb08931.x</identifier><identifier>PMID: 3888625</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Biological and medical sciences ; Catalysis ; Cloning, Molecular ; Dinucleoside Phosphates ; DNA-directed RNA polymerase ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; genes ; Molecular and cellular biology ; Molecular genetics ; Oligonucleotides - metabolism ; Oligoribonucleotides - biosynthesis ; Oxidoreductases Acting on CH-NH Group Donors - biosynthesis ; Oxidoreductases Acting on CH-NH Group Donors - genetics ; Peptide Chain Initiation, Translational ; Ribonucleotides - metabolism ; RNA Polymerase II - metabolism ; Substrate Specificity ; T-Phages - metabolism ; Templates, Genetic ; Transcription, Genetic ; Transcription. Transcription factor. Splicing. Rna processing ; Triticum ; Triticum aestivum ; wheat germ</subject><ispartof>European journal of biochemistry, 1985-01, Vol.149 (2), p.337-343</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5067-75b0677ecd6098865b8959470da983d8d8d9b6e72691e017de9fd6fcdbc074dd3</citedby><cites>FETCH-LOGICAL-c5067-75b0677ecd6098865b8959470da983d8d8d9b6e72691e017de9fd6fcdbc074dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8433714$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3888625$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mosig, H</creatorcontrib><creatorcontrib>Schaffner, A.R</creatorcontrib><creatorcontrib>Sieber, H</creatorcontrib><creatorcontrib>Hartmann, G.R</creatorcontrib><title>Primer-independent abortive initiation by wheat-germ RNA polymerase B (II)</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Highly purified RNA polymerase B (II) from wheat germ catalyses the formation of dinucleoside tetraphosphates from ribonucleoside triphosphates in the absence of an oligonucleotide primer or additional protein factors. The reaction requires bivalent cations such as Mn2+ or Mg2+ and proceeds linearly for several hours. It is strongly inhibited by 1 μg/ml α‐amanitin or 2 μg/ml heparin. The reaction strictly depends on the addition of a specific linear or circular DNA template, such as the plasmid pSmaF or a DNA fragment containing the gene for nopaline dehydrogenase. Bacteriophage T7 D111 DNA has almost no template activity. The start sites for dinucleotide synthesis on the template are limited. With the DNA fragment containing the gene for nopaline dehydrogenase only pppApA and pppApU are synthesised substantially whereas pppUpU is formed only in trace amounts. No significant dinucleotide synthesis is observed with other ribonucleoside triphosphates either singly or in a combination of two. The various regions of the DNA fragment differ distinctly in template activity.</description><subject>Biological and medical sciences</subject><subject>Catalysis</subject><subject>Cloning, Molecular</subject><subject>Dinucleoside Phosphates</subject><subject>DNA-directed RNA polymerase</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Oligonucleotides - metabolism</subject><subject>Oligoribonucleotides - biosynthesis</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - biosynthesis</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - genetics</subject><subject>Peptide Chain Initiation, Translational</subject><subject>Ribonucleotides - metabolism</subject><subject>RNA Polymerase II - metabolism</subject><subject>Substrate Specificity</subject><subject>T-Phages - metabolism</subject><subject>Templates, Genetic</subject><subject>Transcription, Genetic</subject><subject>Transcription. Transcription factor. Splicing. Rna processing</subject><subject>Triticum</subject><subject>Triticum aestivum</subject><subject>wheat germ</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1P2zAUhq0JxLqyn4CI0ITGRYIdx1_cIEBlFCE28XFtOfEJc5UmnZ2u9N_PVaPeTtiSz8X7nvccPwidEJyReM5nGSlonhJMaUaUZFlfYqkoyd4_odFO2kMjjEmR5orxz-hLCDOMMVdcHKADKqXkORuh-1_ezcGnrrWwgPi0fWLKzvfuLySudb0zvevapFwnq99g-vQN_Dx5erxKFl2zjp0mQHKdfJ9Ozw7Rfm2aAF-HOkavt5OXm7v04eeP6c3VQ1oxzEUqWBmLgMpyrOIWrJSKqUJga5SkVsarSg4i54oAJsKCqi2vK1tWWBTW0jE63eYufPdnCaHXcxcqaBrTQrcMWvD4e4XJf42kyHmhuIrGi62x8l0IHmq9iFSMX2uC9Ya4nukNVr3BqjfE9UBcv8fmo2HKspyD3bUOiKP-bdBNqExTe9NWLuxssqBUxPAxutzaVq6B9QcW0LeT6-eYEROOtwm16bR583HI63MeOeCcs7xgiv4D9x2lZQ</recordid><startdate>19850101</startdate><enddate>19850101</enddate><creator>Mosig, H</creator><creator>Schaffner, A.R</creator><creator>Sieber, H</creator><creator>Hartmann, G.R</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19850101</creationdate><title>Primer-independent abortive initiation by wheat-germ RNA polymerase B (II)</title><author>Mosig, H ; Schaffner, A.R ; Sieber, H ; Hartmann, G.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5067-75b0677ecd6098865b8959470da983d8d8d9b6e72691e017de9fd6fcdbc074dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Biological and medical sciences</topic><topic>Catalysis</topic><topic>Cloning, Molecular</topic><topic>Dinucleoside Phosphates</topic><topic>DNA-directed RNA polymerase</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Oligonucleotides - metabolism</topic><topic>Oligoribonucleotides - biosynthesis</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - biosynthesis</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - genetics</topic><topic>Peptide Chain Initiation, Translational</topic><topic>Ribonucleotides - metabolism</topic><topic>RNA Polymerase II - metabolism</topic><topic>Substrate Specificity</topic><topic>T-Phages - metabolism</topic><topic>Templates, Genetic</topic><topic>Transcription, Genetic</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><topic>Triticum</topic><topic>Triticum aestivum</topic><topic>wheat germ</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mosig, H</creatorcontrib><creatorcontrib>Schaffner, A.R</creatorcontrib><creatorcontrib>Sieber, H</creatorcontrib><creatorcontrib>Hartmann, G.R</creatorcontrib><collection>AGRIS</collection><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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mosig, H</au><au>Schaffner, A.R</au><au>Sieber, H</au><au>Hartmann, G.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Primer-independent abortive initiation by wheat-germ RNA polymerase B (II)</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1985-01-01</date><risdate>1985</risdate><volume>149</volume><issue>2</issue><spage>337</spage><epage>343</epage><pages>337-343</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>Highly purified RNA polymerase B (II) from wheat germ catalyses the formation of dinucleoside tetraphosphates from ribonucleoside triphosphates in the absence of an oligonucleotide primer or additional protein factors. The reaction requires bivalent cations such as Mn2+ or Mg2+ and proceeds linearly for several hours. It is strongly inhibited by 1 μg/ml α‐amanitin or 2 μg/ml heparin. The reaction strictly depends on the addition of a specific linear or circular DNA template, such as the plasmid pSmaF or a DNA fragment containing the gene for nopaline dehydrogenase. Bacteriophage T7 D111 DNA has almost no template activity. The start sites for dinucleotide synthesis on the template are limited. With the DNA fragment containing the gene for nopaline dehydrogenase only pppApA and pppApU are synthesised substantially whereas pppUpU is formed only in trace amounts. No significant dinucleotide synthesis is observed with other ribonucleoside triphosphates either singly or in a combination of two. The various regions of the DNA fragment differ distinctly in template activity.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>3888625</pmid><doi>10.1111/j.1432-1033.1985.tb08931.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Biological and medical sciences Catalysis Cloning, Molecular Dinucleoside Phosphates DNA-directed RNA polymerase Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Fundamental and applied biological sciences. Psychology genes Molecular and cellular biology Molecular genetics Oligonucleotides - metabolism Oligoribonucleotides - biosynthesis Oxidoreductases Acting on CH-NH Group Donors - biosynthesis Oxidoreductases Acting on CH-NH Group Donors - genetics Peptide Chain Initiation, Translational Ribonucleotides - metabolism RNA Polymerase II - metabolism Substrate Specificity T-Phages - metabolism Templates, Genetic Transcription, Genetic Transcription. Transcription factor. Splicing. Rna processing Triticum Triticum aestivum wheat germ |
title | Primer-independent abortive initiation by wheat-germ RNA polymerase B (II) |
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