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- W22022962 endingPage "69" @default.
- W22022962 startingPage "53" @default.
- W22022962 abstract "Human topoisomerase I (Top1) catalyzes the reversible cleavage of one strand of DNA to provide swivels to relax the supercoils associated with DNA replication, transcription, and chromatin assembly. The cleavage reaction occurs with the covalent attachment of an active-site tyrosine to the 3′ end of the broken strand; religation restores continuity to the DNA and releases the enzyme. During the cleaved state, relaxation of torsionally strained supercoils occurs by a controlled rotation mechanism. X-ray crystal structures of the enzyme with bound DNA combined with single-molecule experiments provide insights into the chemistry, specificity, and dynamics of the DNA relaxation process. A failure of Top1 to carry out religation at DNA lesions or in the presence of drugs such as camptothecin causes DNA damage that must be repaired if the cell is to survive. The list of proteins known to interact with Top1 suggests that the enzyme has functions in vivo that extend well beyond the previously characterized roles in replication, transcription, and chromatin assembly." @default.
- W22022962 created "2016-06-24" @default.
- W22022962 creator A5032960501 @default.
- W22022962 date "2011-08-26" @default.
- W22022962 modified "2023-09-23" @default.
- W22022962 title "Human DNA Topoisomerase I: Structure, Enzymology and Biology" @default.
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