Orchestrating serine resolvases.
Orchestrating serine resolvases.
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协调丝氨酸解析酶。
DOI：
10.1042/bst0380384
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发表时间：
2010
影响因子：
3.9
通讯作者：
Stark,WMarshall
中科院分区：
文献类型：
--
作者：
Rice,PhoebeA;Mouw,KentW;Montaño,SherwinP;Boocock,MartinR;Rowland,Sally-J;Stark,WMarshall
丝氨酸分解酶的一个显著特征是它们的调节：野生型酶将催化分子内而不是分子间的重组，可以感知它们位点的相对方向，并且可以定向地交换链，尽管事实上没有化学键能的净释放。这种调节的关键是它们只在一个称为“突触体”的大型交织复合体中活跃。由于基底拓扑结构极大地促进（或在其他情况下，抑制）突触体的形成，因此它充当“拓扑过滤器”。在突触体的定义拓扑结构内，链交换释放超螺旋张力，提供能量源以偏置反应方向。该复合物的调节部分含有重组酶的额外拷贝，有时还含有其他DNA弯曲蛋白。我们正在使用X射线晶体学，生物化学和遗传学的组合来模拟完整的突触复合体，并了解调控部分如何激活交叉位点结合的重组酶。
A remarkable feature of the serine resolvases is their regulation: the wild-type enzymes will catalyse intra- but not inter-molecular recombination, can sense the relative orientation of their sites and can exchange strands directionally, despite the fact that there is no net release of chemical bond energy. The key to this regulation is that they are only active within a large intertwined complex called the ‘synaptosome’. Because substrate topology greatly facilitates (or, in other cases, inhibits) formation of the synaptosome, it acts as a ‘topological filter’. Within the defined topology of the synaptosome, strand exchange releases supercoiling tension, providing an energy source to bias the reaction direction. The regulatory portion of this complex contains additional copies of the recombinase and sometimes other DNA-bending proteins. We are using a combination of X-ray crystallography, biochemistry and genetics to model the full synaptic complex and to understand how the regulatory portion activates the crossover-site-bound recombinases.