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. 1992 Mar 1;89(5):1524–1528. doi: 10.1073/pnas.89.5.1524

Functional complementation of internal deletion mutants in the lactose permease of Escherichia coli.

E Bibi 1, H R Kaback 1
PMCID: PMC48484  PMID: 1542643

Abstract

Using the lactose permease of Escherichia coli, a well-characterized membrane protein with 12 transmembrane domains, we demonstrated that certain paired in-frame deletion constructs complement each other functionally. Although cells expressing the deletion mutants individually are unable to catalyze active lactose accumulation, cells simultaneously expressing specific pairs of deletions catalyze transport up to 60% as do cells expressing wild-type permease. Moreover, complementation clearly does not occur at the level of DNA but probably occurs at the protein level. Remarkably, functional complementation is observed only with pairs of permease molecules containing large deletions and is not observed with missense mutations or point deletions. Although the mechanism of functional complementation is obscure, the findings indicate that certain pairs of permease molecules containing specific internal deletions can interact to form a functional complex in the same way phenomenologically as do independently expressed polypeptides corresponding to different N- and C-terminal portions of the permease.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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