AMINO-ACID SEQUENCE FOR PEPTIDE EXTENSION ON PRO-LIPOPROTEIN OF ESCHERICHIA-COLI OUTER MEMBRANE
AMINO-ACID SEQUENCE FOR PEPTIDE EXTENSION ON PRO-LIPOPROTEIN OF ESCHERICHIA-COLI OUTER MEMBRANE
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DOI：
10.1073/pnas.74.3.1004
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发表时间：
1977-01-01
影响因子：
11.1
通讯作者：
INOUYE, M
中科院分区：
文献类型：
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作者：
INOUYE, S;WANG, S;INOUYE, M
大肠杆菌外膜脂蛋白的mRNA编码一个假定的前体，原脂蛋白，它有20个额外的氨基酸残基从脂蛋白的氨基端延伸出来。以纯化的脂蛋白mRNA为导向，在大肠杆菌无细胞体系中合成的原脂蛋白，其氨基末端前体区完整氨基酸序列如下：**GRAPHIC**。在甲苯处理的细胞中积累的原脂蛋白具有相同的序列。从脂蛋白在大肠杆菌外膜生物合成和组装的机制方面讨论了氨基酸序列的意义。
The mRNA for the lipoprotein of the E. coli outer membrane coded for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified mRNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was as follows: .**GRAPHIC**. The prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.