Identification of a Minimal Functional Linker in Human Topoisomerase I by Domain Swapping with Cre Recombinase
| Autor: | Rikke Frøhlich, Christopher Veigaard, Sissel Juul, Marianne Smedegaard Hede, Maria Vinther, Felicie F. Andersen, Maria Bjerre Nielsen |
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| Rok vydání: | 2008 |
| Předmět: |
Cre recombinase
Sodium Chloride Biology Biochemistry Protein Structure Secondary Structure-Activity Relationship Protein structure Recombinase Humans Tyrosine Floxing chemistry.chemical_classification Integrases Topoisomerase DNA Hydrogen Peroxide Molecular biology Recombinant Proteins Protein Structure Tertiary Amino acid Cell biology DNA Topoisomerases Type I chemistry biology.protein Camptothecin Linker |
| Zdroj: | Hougaard, R F, Juul, S, Vinther, M, Veigaard, C, Hede, M S & Andersen, F F 2008, ' Identification of a minimal functional linker in human topoisomerase I by domain swapping with Cre recombinase ', Biochemistry, vol. 47, no. 27, pp. 7127-7136 . https://doi.org/10.1021/bi800031k |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi800031k |
| Popis: | Cellular forms of type IB topoisomerases distinguish themselves from their viral counterparts and the tyrosine recombinases to which they are closely related by having rather extensive N-terminal and linker domains. The functions and necessity of these domains are not yet fully unraveled. In this study we replace 86 amino acids including the linker domain of the cellular type IB topoisomerase, human topoisomerase I, with four, six, or eight amino acids from the corresponding short loop region in Cre recombinase. In vitro characterization of the resulting chimeras, denoted Cropos, reveals that six amino acids from the Cre linker loop constitute the minimal length of a functional linker in human topoisomerase I. |
| Databáze: | OpenAIRE |
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