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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...

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Detalles Bibliográficos
Autor principal: Ho, P Shing
Formato: Texto
Lenguaje:English
Publicado: Biology Reports Ltd 2009
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