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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
45
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pubmed:dateCreated |
2003-11-3
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pubmed:abstractText |
DnaE-type DNA polymerases belong to the C family of DNA polymerases and are responsible for chromosomal replication in prokaryotes. Like most closely related Gram-positive cells, Streptococcus pyogenes has two DnaE homologs Pol C and DnaE; both are essential to cell viability. Pol C is an established replicative polymerase, and DnaE has been proposed to serve a replicative role. In this report, we characterize S. pyogenes DnaE polymerase and find that it is highly error-prone. DnaE can bypass coding and noncoding lesions with high efficiency. Error-prone extension is accomplished by either of two pathways, template-primer misalignment or direct primer extension. The bypass of abasic sites is accomplished mainly through "dNTP-stabilized" misalignment of template, thereby generating (-1) deletions in the newly synthesized strand. This mechanism may be similar to the dNTP-stabilized misalignment mechanism used by the Y family of DNA polymerases and is the first example of lesion bypass and error-prone synthesis catalyzed by a C family polymerase. Thus, DnaE may function in an error-prone capacity that may be essential in Gram-positive cells but not Gram-negative cells, suggesting a fundamental difference in DNA metabolism between these two classes of bacteria.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-Aminopurine,
http://linkedlifedata.com/resource/pubmed/chemical/8-oxo-7-hydrodeoxyguanosine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase III,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA polymerase III, alpha subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyguanosine,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Thymine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/dnaQ protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/thymidine 5'-triphosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44361-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12949067-2-Aminopurine,
pubmed-meshheading:12949067-Base Pair Mismatch,
pubmed-meshheading:12949067-Base Sequence,
pubmed-meshheading:12949067-DNA,
pubmed-meshheading:12949067-DNA Polymerase III,
pubmed-meshheading:12949067-DNA Primers,
pubmed-meshheading:12949067-Deoxyguanosine,
pubmed-meshheading:12949067-Escherichia coli,
pubmed-meshheading:12949067-Escherichia coli Proteins,
pubmed-meshheading:12949067-Kinetics,
pubmed-meshheading:12949067-Oligonucleotides,
pubmed-meshheading:12949067-Streptococcus pyogenes,
pubmed-meshheading:12949067-Substrate Specificity,
pubmed-meshheading:12949067-Templates, Genetic,
pubmed-meshheading:12949067-Thymine Nucleotides
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pubmed:year |
2003
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pubmed:articleTitle |
The essential C family DnaE polymerase is error-prone and efficient at lesion bypass.
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pubmed:affiliation |
The Rockefeller University, New York, New York 10021, USA. bruck@mod.rockefeller.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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