Ontology highlight
ABSTRACT:
SUBMITTER: Bibi E
PROVIDER: S-EPMC48484 | biostudies-other | 1992 Mar
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 19920301 5
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 ...[more]