Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B
Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B
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DOI：
10.1046/j.1432-1327.2001.02091.x
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发表时间：
2001-04-01
期刊：
影响因子：
--
通讯作者：
Shaw, PC
中科院分区：
文献类型：
--
作者：
Chan, SH;Hung, FSJ;Shaw, PC
天花粉蛋白是一种核糖体失活蛋白，具有多种药理学特性。通过酵母双杂交系统，核糖体磷蛋白P0和P1和一个假定的有丝分裂检查点蛋白，MAD 2B，被发现与活性位点突变的天花粉蛋白（TCS）相互作用。通过重组野生型TCS和靶蛋白的体外结合试验验证了相互作用。PO的相互作用结构域被定位于氨基酸220-273，这是先前报道的参与与P1和P2在酵母中的相互作用。与我们先前的发现一致，TCS的最后7个残基对于活性构象不是必需的，相同的缺失不影响与P0的相互作用。我们目前的研究表明，TCS可能会破坏延伸因子的P-复合物的结合，除了众所周知的核糖体失活的N-糖苷酶活性。
Trichosanthin is a ribosome-inactivating protein with multiple pharmacological properties. By a yeast two-hybrid system, ribosomal phosphoproteins P0 and P1 and a putative mitotic checkpoint protein, MAD2B, were found to interact with an active-site mutated trichosanthin (TCS). The interactions were verified by an in vitro binding assay of recombinant wild-type TCS and target proteins. The interaction domain of PO was mapped to amino acids 220-273, which had been previously reported to be involved in the interaction with P1 and P2 in yeast. Consistent with our previous finding that the last seven residues of TCS are not essential for an active conformation, the same deletion did not affect the interaction with P0. Our present study suggests that TCS may disrupt the binding of elongation factors to the P-complex, in addition to the well-known N-glycosidase activity for ribosome inactivation.