Yang J Y, Jayaram M, Harshey R M
Department of Microbiology, University of Texas at Austin, 78712, USA.
Cell. 1996 May 3;85(3):447-55. doi: 10.1016/s0092-8674(00)81122-8.
The strand cleavage and strand transfer reactions of Mu DNA transposition require structural/catalytic contributions from separate polypeptide domains of individual transposase (MuA) monomers within the functional MuA tetramer. Based on catalytic complementation between two inactive MuA variants, we have derived certain rules by which the physical location of a MuA monomer within the transposition complex specifies its role in DNA breakage and transfer. During strand transfer, MuA monomers contributing domain II to the reaction occupy R1 (the subsite proximal to the strand-transferred nucleotide), while those contributing domain IIIalpha occupy R2. The positions of the monomers contributing these two domains appear to be reversed during DNA cleavage.
Mu DNA转座过程中的链切割和链转移反应需要功能性MuA四聚体内单个转座酶（MuA）单体的不同多肽结构域提供结构/催化作用。基于两个无活性MuA变体之间的催化互补作用，我们得出了一些规则，根据这些规则，转座复合物中MuA单体的物理位置决定了其在DNA断裂和转移中的作用。在链转移过程中，为反应提供结构域II的MuA单体占据R1（靠近链转移核苷酸的亚位点），而提供结构域IIIα的单体占据R2。在DNA切割过程中，提供这两个结构域的单体位置似乎发生了反转。
