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Tn5 synaptic complex formation : role of transposase residue W450
Authors
Richard J. Gradman
William S. Reznikoff
Publication date
14 December 2007
Publisher
'American Society for Microbiology'
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PubMed
Abstract
Author Posting. © American Society for Microbiology, 2008. This article is posted here by permission of American Society for Microbiology for personal use, not for redistribution. The definitive version was published in Journal of Bacteriology 190 (2008): 1484-1487, doi:10.1128/JB.01488-07.A series of Tn5 transposases (Tnp's) with mutations at the conserved amino acid position W450, which was structurally predicted to be important for synapsis, have been generated and characterized. This study demonstrates that W450 is involved in hydrophobic (and possibly aromatic) contacts within the Tnp monomer that negatively regulate synaptic complex formation.This work was supported by the NIH (grant no. GM50693) and the University of Wisconsin—Madison (grant no. WIS04792) and through the Evelyn Mercer Professorship in Biochemistry and Molecular Biology
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