Manna Baisali, Bhattacharya Tanusree, Kahali Bratati, Ghosh Tapash Chandra
Bioinformatics Centre, Bose Institute, P 1/12, C.I.T. Scheme VII M, Kolkata-700 054, India.
Gene. 2009 Apr 1;434(1-2):50-5. doi: 10.1016/j.gene.2008.12.013. Epub 2008 Dec 29.
It has been claimed that proteins with more interacting partners (hubs) are structurally more disordered and have a slow evolutionary rate. Here, in this paper we analyzed the evolutionary rate and structural disorderness of human hub and non-hub proteins present/absent in protein complexes. We observed that both non-hub and hub proteins present in protein complexes, are characterized by high structural disorderness. There exists no significant difference in average evolutionary rate of complex-forming hub and non-hub proteins while we have found a significant difference in the average evolutionary rate between hub and non-hub proteins which are not present in protein complexes. We concluded that higher disorderness in complex forming non-hub proteins facilitates higher number of interactions with a large number of protein subunits. High interaction among protein subunits of complex forming non-hub proteins imposes a selective constraint on their evolutionary rate.
有人声称，具有更多相互作用伙伴（枢纽蛋白）的蛋白质在结构上更无序，进化速率较慢。在此，我们分析了蛋白质复合物中存在/不存在的人类枢纽蛋白和非枢纽蛋白的进化速率和结构无序性。我们观察到，蛋白质复合物中存在的非枢纽蛋白和枢纽蛋白均具有高度的结构无序性。形成复合物的枢纽蛋白和非枢纽蛋白的平均进化速率没有显著差异，而我们发现不在蛋白质复合物中的枢纽蛋白和非枢纽蛋白的平均进化速率存在显著差异。我们得出结论，形成复合物的非枢纽蛋白中较高的无序性促进了与大量蛋白质亚基的更多相互作用。形成复合物的非枢纽蛋白的蛋白质亚基之间的高相互作用对其进化速率施加了选择性限制。
