PMID:7961482
| Citation |
Kimbrough, TG and Manoil, C (1994) Role of a small cytoplasmic domain in the establishment of serine chemoreceptor membrane topology. J. Bacteriol. 176:7118-20 |
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| Abstract |
The Escherichia coli serine chemoreceptor takes on a simple membrane topology with two transmembrane segments separating cytoplasmically disposed N and C termini from a central periplasmic domain. We investigated the role of the small N-terminal cytoplasmic domain in membrane insertion using alkaline phosphatase gene fusions. Mutations eliminating the positive charge of the domain altered insertion dramatically, with reciprocal effects on hybrids with periplasmic and C-terminal cytoplasmic fusion junctions. Efficient export of the normally cytoplasmic C-terminal domain required that, in addition to the N-terminal changes, a short amphiphatic sequence at the beginning of the C-terminal domain be also absent. These findings document the importance of the positive character of the N-terminal domain in chemoreceptor membrane insertion and imply that partially redundant sequence information controls the orientation of the second transmembrane segment. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Escherichia coli/chemistry; Escherichia coli/genetics; Membrane Proteins/chemistry; Membrane Proteins/genetics; Molecular Conformation; Molecular Sequence Data; Peptide Fragments/chemistry; Receptors, Cytoplasmic and Nuclear/chemistry; Recombinant Fusion Proteins/chemistry; Serine/metabolism |
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