Source:http://linkedlifedata.com/resource/pubmed/id/15200644
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-6-17
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pubmed:abstractText |
Cell survival after DNA damage depends on specialized DNA polymerases able to perform DNA synthesis on imperfect templates. Most of these enzymes belong to the recently discovered Y-family of DNA polymerases, none of which has been previously described in plants. We report here the isolation, functional characterization and expression analysis of a plant representative of the Y-family. This polymerase, which we have termed AtPolkappa, is a homolog of Escherichia coli pol IV and human pol kappa, and thus belongs to the DinB subfamily. We purified AtPolkappa and found a template-directed DNA polymerase, endowed with limited processivity that is able to extend primer-terminal mispairs. The activity and processivity of AtPolkappa are enhanced markedly upon deletion of 193 amino acids (aa) from its carboxy (C)-terminal domain. Loss of this region also affects the nucleotide selectivity of the enzyme, leading to the incorporation of both dCTP and dTTP opposite A in the template. We detected three cDNA forms, which result from the alternative splicing of AtPOLK mRNA and have distinct patterns of expression in different plant organs. Histochemical localization of beta-glucuronidase (GUS) activity in transgenic plants revealed that the AtPOLK promoter is active in endoreduplicating cells, suggesting a possible role during consecutive DNA replication cycles in the absence of mitosis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
84-97
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15200644-Alternative Splicing,
pubmed-meshheading:15200644-Amino Acid Sequence,
pubmed-meshheading:15200644-Arabidopsis,
pubmed-meshheading:15200644-Arabidopsis Proteins,
pubmed-meshheading:15200644-DNA-Directed DNA Polymerase,
pubmed-meshheading:15200644-Gene Expression,
pubmed-meshheading:15200644-Gene Library,
pubmed-meshheading:15200644-Molecular Sequence Data,
pubmed-meshheading:15200644-Phylogeny,
pubmed-meshheading:15200644-Plants, Genetically Modified,
pubmed-meshheading:15200644-Recombinant Fusion Proteins,
pubmed-meshheading:15200644-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Arabidopsis thaliana AtPOLK encodes a DinB-like DNA polymerase that extends mispaired primer termini and is highly expressed in a variety of tissues.
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pubmed:affiliation |
Departamento de Genética, Universidad de Córdoba, 14071 Córdoba, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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