Skvirsky R C, Shen X, Reginald S
Department of Biology, University of Massachusetts Boston 02125, USA.
FEMS Microbiol Lett. 1996 May 1;138(2-3):201-6. doi: 10.1111/j.1574-6968.1996.tb08157.x.
The antibacterial peptide toxin colicin V is exported from Escherichia coli cells by a signal sequence-independent, ABC export system. Export requires at least three proteins-membrane fusion protein CvaA, ABC export protein CvaB, and outer membrane protein TolC. The cvaA gene also encodes a second protein, CvaA, initiated from an in-frame translational re-start within the cvaA coding sequence. To determine whether the internally encoded CvaA protein also functions in the export pathway, the putative start codons for CvaA were mutagenized, while maintaining CvaA function. Elimination of CvaA translation caused no change in colicin V export levels, indicating that the CvaA protein is not required in the secretion pathway.
抗菌肽毒素大肠杆菌素V通过一个不依赖信号序列的ABC输出系统从大肠杆菌细胞中输出。输出至少需要三种蛋白质——膜融合蛋白CvaA、ABC输出蛋白CvaB和外膜蛋白TolC。cvaA基因还编码第二种蛋白CvaA,它起始于cvaA编码序列内的一个框内翻译重新起始。为了确定内部编码的CvaA蛋白是否也在输出途径中发挥作用,在保持CvaA功能的同时,对CvaA的推定起始密码子进行了诱变。消除CvaA的翻译对大肠杆菌素V的输出水平没有影响,表明分泌途径中不需要CvaA蛋白。