Source:http://linkedlifedata.com/resource/pubmed/id/10585475
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2000-1-13
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pubmed:abstractText |
The primase fragment of bacteriophage T7 gene 4 protein catalyzes the synthesis of oligoribonucleotides in the presence of ATP, CTP, Mg(2+) (or Mn(2+)), and DNA containing a primase recognition site. During chain initiation, ATP binds with a K(m) of 0.32 mM, and CTP binds with a K(m) of 0.85 mM. Synthesis of the dinucleotides proceeds at a rate of 3.8/s. The dinucleotide either dissociates or is extended to a tetranucleotide. The primase preferentially inserts ribonucleotides forming Watson-Crick base pairs with the DNA template >200-fold more rapidly than other ribo- or deoxynucleotides. 3'-dCTP binds the primase with a similar affinity as CTP and is incorporated as a chain terminator at a rate (1)/(100) that of CTP. ATP analogues alpha,beta-methylene ATP, beta,gamma-methylene ATP, and beta,gamma-imido ATP are incorporated by the primase fragment at the 5'-ends of the oligoribonucleotides but not at the 3'-ends. A model is presented in which the primase fragment utilizes two nucleotide-binding sites, one for the initiating ATP and one for the nucleoside triphosphate which elongates the primer on the 3'-end. The initiation site binds ATP or oligoribonucleotides, whereas the elongation site binds ATP or CTP as directed by the template.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cytidine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primase,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligoribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35899-907
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10585475-Adenosine Triphosphate,
pubmed-meshheading:10585475-Bacteriophage T7,
pubmed-meshheading:10585475-Base Sequence,
pubmed-meshheading:10585475-Binding Sites,
pubmed-meshheading:10585475-Cytidine Triphosphate,
pubmed-meshheading:10585475-DNA Primase,
pubmed-meshheading:10585475-Kinetics,
pubmed-meshheading:10585475-Magnesium Chloride,
pubmed-meshheading:10585475-Manganese,
pubmed-meshheading:10585475-Oligodeoxyribonucleotides,
pubmed-meshheading:10585475-Oligoribonucleotides,
pubmed-meshheading:10585475-Ribonucleotides,
pubmed-meshheading:10585475-Substrate Specificity,
pubmed-meshheading:10585475-Templates, Genetic
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pubmed:year |
1999
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pubmed:articleTitle |
Interaction of ribonucleoside triphosphates with the gene 4 primase of bacteriophage T7.
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pubmed:affiliation |
Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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