Kim J, Luirink J, Kendall D A
Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269, USA.
J Bacteriol. 2000 Jul;182(14):4108-12. doi: 10.1128/JB.182.14.4108-4112.2000.
We have used Escherichia coli alkaline phosphatase to show the interplay among the characteristics of two amino-terminal domains in the preprotein (the signal peptide and the early mature region), the efficiency with which this protein is transported, and its requirement for SecB to accomplish the transport process. The results suggest that although alkaline phosphatase does not normally require SecB for transport, it is inherently able to utilize SecB, and it does so when its ability to interface with the transport machinery is compromised.
我们利用大肠杆菌碱性磷酸酶来展示前体蛋白中两个氨基末端结构域(信号肽和早期成熟区域)的特征、该蛋白的转运效率以及其完成转运过程对SecB的需求之间的相互作用。结果表明,尽管碱性磷酸酶正常情况下转运不需要SecB,但它本身能够利用SecB,并且当其与转运机制相互作用的能力受损时就会这样做。