Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B
Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B
复制标题
大肠杆菌中 CyaA-PrtB 和 HlyA-PrtB 融合蛋白的分泌：菊欧文氏菌蛋白酶 B 富含甘氨酸的重复结构域的参与
DOI：
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发表时间：
1992
影响因子：
3.2
通讯作者：
C. Wandersman
中科院分区：
文献类型：
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作者：
S. Létoffé;C. Wandersman
先前表明，来自菊欧文氏菌的蛋白酶 B 具有位于包含六个富含甘氨酸重复序列的结构域下游的 C 末端分泌信号。该结构域在所有已知的由信号肽独立途径分泌的细菌蛋白中都是保守的。这些重复序列在分泌过程中的作用是有争议的。我们比较了直接与信号融合或通过富含甘氨酸结构域与其分离的各种异源多肽的分泌过程。尽管重复序列不参与小截短蛋白酶 B 羧基端肽的分泌，但它们是分泌较高分子量融合蛋白所必需的。分泌效率还取决于过客多肽的大小。
Protease B from Erwinia chrysanthemi was shown previously to have a C-terminal secretion signal located downstream of a domain that contains six glycine-rich repeats. This domain is conserved in all known bacterial proteins secreted by the signal peptide-independent pathway. The role of these repeats in the secretion process is controversial. We compared the secretion processes of various heterologous polypeptides fused either directly to the signal or separated from it by the glycine-rich domain. Although the repeats are not involved in the secretion of small truncated protease B carboxy-terminal peptides, they are required for the secretion of higher-molecular-weight fusion proteins. Secretion efficiency was also dependent on the size of the passenger polypeptide.