ArticleReports of biochemistry & molecular biology2020
Swapping of The N-Terminal Domain of Human Topoisomerase 1B with the Corresponding
Article in Reports of biochemistry & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors at 2 institutions in 1 country.
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Abstract
backgroundDNA topoisomerases 1B are a class of ubiquitous enzyme that solves the topological problems associated with biological processes such as replication, transcription and recombination. Numerous sequence alignment of topoisomerase 1B from different species shows that the lengths of different domains as well as their amino acids sequences are quite different. In the present study a hybrid enzyme, generated by swapping the N-terminal of
methodsThe chimeric enzyme was generated using different sets of PCR. The
resultsThe chimeric enzyme displayed slower relaxation activity, cleavage and re-ligation kinetics strongly perturbed when compared to the human enzyme.
conclusionThese results indicate that the N-terminal domain has a crucial role in modulating topoisomerase activity in different species.
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Identifiers
32582794PMC7275839W3030592857What OpenQuestion holds
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