18849470

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012892, umls-concept:C0012929, umls-concept:C0064360, umls-concept:C0598312, umls-concept:C1514873, umls-concept:C1546857, umls-concept:C1556066, umls-concept:C1619636
pubmed:issue	12
pubmed:dateCreated	2008-12-5
pubmed:abstractText	Kinetoplast DNA (kDNA), the mitochondrial genome of trypanosomes, is a catenated network containing thousands of minicircles and tens of maxicircles. The topological complexity dictates some unusual features including a topoisomerase-mediated release-and-reattachment mechanism for minicircle replication and at least six mitochondrial DNA polymerases (Pols) for kDNA transactions. Previously, we identified four family A DNA Pols from Trypanosoma brucei with similarity to bacterial DNA Pol I and demonstrated that two (POLIB and POLIC) were essential for maintaining the kDNA network, while POLIA was not. Here, we used RNA interference to investigate the function of POLID in procyclic T. brucei. Stem-loop silencing of POLID resulted in growth arrest and the progressive loss of the kDNA network. Additional defects in kDNA replication included a rapid decline in minicircle and maxicircle abundance and a transient accumulation of minicircle replication intermediates before loss of the kDNA network. These results demonstrate that POLID is a third essential DNA Pol required for kDNA replication. While other eukaryotes utilize a single DNA Pol (Pol gamma) for replication of mitochondrial DNA, T. brucei requires at least three to maintain the complex kDNA network.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/AI066279
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101130731
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/DNA, Kinetoplast, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase, http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1535-9786
pubmed:author	pubmed-author:ChandlerJulianJ, pubmed-author:KlingbeilMichele MMM, pubmed-author:MozeleskiBrianB, pubmed-author:VandorosAnthula VAV
pubmed:issnType	Electronic
pubmed:volume	7
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	2141-6
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:18849470-Animals, pubmed-meshheading:18849470-DNA, Kinetoplast, pubmed-meshheading:18849470-DNA Replication, pubmed-meshheading:18849470-DNA-Directed DNA Polymerase, pubmed-meshheading:18849470-Mitochondria, pubmed-meshheading:18849470-Mitochondrial Proteins, pubmed-meshheading:18849470-Protozoan Proteins, pubmed-meshheading:18849470-RNA, Double-Stranded, pubmed-meshheading:18849470-RNA Interference, pubmed-meshheading:18849470-Trypanosoma brucei brucei
pubmed:year	2008
pubmed:articleTitle	Stem-loop silencing reveals that a third mitochondrial DNA polymerase, POLID, is required for kinetoplast DNA replication in trypanosomes.
pubmed:affiliation	Department of Microbiology, University of Massachusetts, 639 North Pleasant Street, Amherst, MA 01003, USA.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural