Source:http://linkedlifedata.com/resource/pubmed/id/15830206
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-7-15
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pubmed:abstractText |
Human DNA topoisomerase I is an essential enzyme involved in resolving the torsional stress associated with DNA replication, transcription, and chromatin condensation. The catalytic cycle of the enzyme consists of DNA cleavage to form a covalent enzyme-DNA intermediate, DNA relaxation, and finally, re-ligation of the phosphate backbone to restore the continuity of the DNA. Structure/function studies have elucidated a flexible enzyme that relaxes DNA through coordinated, controlled movements of distinct enzyme domains. The cellular roles of topoisomerase I are apparent throughout the nucleus, but the concentration of processes acting on ribosomal DNA results in topoisomerase I accumulation in the nucleolus. Although the activity of topoisomerase I is required in these processes, the enzyme can also have a deleterious effect on cells. In the event that the final re-ligation step of the reaction cycle is prevented, the covalent topoisomerase I-DNA intermediate becomes a toxic DNA lesion that must be repaired. The complexities of the relaxation reaction, the cellular roles, and the pathways that must exist to repair topoisomerase I-mediated DNA damage highlight the importance of continued study of this essential enzyme.
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pubmed:grant | |
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 |
0009-5915
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
75-85
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15830206-DNA Damage,
pubmed-meshheading:15830206-DNA Replication,
pubmed-meshheading:15830206-DNA Topoisomerases, Type I,
pubmed-meshheading:15830206-Humans,
pubmed-meshheading:15830206-Models, Biological,
pubmed-meshheading:15830206-Models, Molecular,
pubmed-meshheading:15830206-Protein Conformation
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pubmed:year |
2005
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pubmed:articleTitle |
Human DNA topoisomerase I: relaxation, roles, and damage control.
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pubmed:affiliation |
Department of Microbiology, School of Medicine, University of Washington, P.O. Box 357242, 1959 N.E. Pacific St., Seattle, WA 98195-7242, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, N.I.H., Extramural
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