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Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex
A series of single-crystal structures determined by Barabas and colleagues provides a detailed mechanism for how the TnpA transposase from Helicobacter pylori recognizes, cleaves, and integrates the IS200/IS605 class of transposable elements. An interesting aspect of the mechanism is that the transp...
Autor principal: | Ho, P Shing |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Biology Reports Ltd
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924686/ https://www.ncbi.nlm.nih.gov/pubmed/20948648 http://dx.doi.org/10.3410/B1-37 |
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