Gradman Richard J, Reznikoff William S
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
J Bacteriol. 2008 Feb;190(4):1484-7. doi: 10.1128/JB.01488-07. Epub 2007 Dec 14.
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.
已构建并鉴定了一系列在保守氨基酸位置W450处发生突变的Tn5转座酶(Tnp's),从结构上预测该位置对突触形成很重要。这项研究表明,W450参与Tnp单体内部的疏水(可能还有芳香)接触,这些接触对突触复合物的形成起负调控作用。