期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：10
页码：4891-4895
DOI：10.1073/pnas.75.10.4891
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Lipoprotein has been purified from an Escherichia coli strain carrying a mutation in the structural gene for murein lipoprotein (mlpA). Amino acid analysis of the purified mutant lipoprotein indicates that the mutant lipoprotein corresponds to the uncleaved prolipoprotein with a single amino acid replacement of glycine with aspartic acid. Automated Edman degradation has established the precise location of this amino acid substitution to be at the 14th residue of the prolipoprotein. This alteration in the signal sequence of prolipoprotein results in a failure of the mutated prolipoprotein to be processed. Furthermore, the structural alteration in the mutant lipoprotein appears also to have affected its topological localization in the mutant cell. Whereas lipoprotein in the wild-type strain is exclusively located in the outer membrane of the cell envelope, the membrane-bound lipoprotein in this mutant is recovered in both the inner and outer membranes of the cell envelope. The data suggest, however, that proteolytic cleavage of prolipoprotein to form mature lipoprotein is not essential for the translocation and assembly of lipoprotein into the outer membrane.
