The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization.
The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization.
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DOI：
10.1111/j.1574-6968.2011.02478.x
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发表时间：
2012-02
影响因子：
2.1
通讯作者：
Xueling Shen;Shan-Zhen Li;Yiling Du;X. Mao;Yongquan Li
中科院分区：
文献类型：
--
作者：
Xueling Shen;Shan-Zhen Li;Yiling Du;X. Mao;Yongquan Li
FtsY is the receptor of the signal recognition particle that mediates the targeting of integral membrane proteins in bacteria. It was shown that in Escherichia coli, the N-terminal region of FtsY contributes to its interaction with the membrane, but it is not inserted into the membrane. However, this study presents evidence that in Streptomyces coelicolor, FtsY has a hydrophobic region at its N-terminus, which forms a membrane insertion structure and contributes significantly to the binding between FtsY and membrane. Through membrane protein extraction followed by immunoblotting, we demonstrated that deletion of the N-terminal residues 11-39 from the S. coelicolor FtsY (ScFtsY) drastically reduced its membrane-binding capability and that the N-terminus of ScFtsY alone was capable of targeting the soluble EGFP protein onto the membrane with high efficiency. Furthermore, in a labeling experiment with the membrane-impermeable probe Mal-PEG, the ScFtsY N-terminal region was protected by the membrane and was not labeled. This observation indicates that this region was inserted into the membrane.
