Structure/function insights into Tn5 transposition.

Mindy Steiniger-White; Ivan Rayment; William S Reznikoff

doi:10.1016/j.sbi.2004.01.008

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Structure/function insights into Tn5 transposition.

Mindy Steiniger-White·Ivan Rayment·William S Reznikoff

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Abstract

Prokaryotic transposon 5 (Tn5) serves as a model system for studying the molecular mechanism of DNA transposition. Elucidation of the X-ray co-crystal structure of Tn5 transposase complexed with a DNA recognition end sequence provided the first three-dimensional picture of an intermediate in a transposition/retroviral integration pathway. The many Tn5 transposase-DNA co-crystal structures now available complement biochemical and genetic studies, allowing a comprehensive and detailed understanding of transposition mechanisms. Specifically, the structures reveal two different types of protein-DNA contacts: cis contacts, required for initial DNA recognition, and trans contacts, required for catalysis. Protein-protein contacts required for synapsis are also seen. Finally, the two divalent metals in the active site of the transposase support a 'two-metal-ion' mechanism for Tn5 transposition.

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Catalysis DNA DNA Transposable Elements Models, Molecular Nucleic Acid Conformation Protein Binding Protein Conformation Structure-Activity Relationship Transposases Journal Article Review

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Mindy Steiniger-White, Ivan Rayment, William S Reznikoff. 2004. Structure/function insights into Tn5 transposition.. https://doi.org/10.1016/j.sbi.2004.01.008

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