Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
Journal Article
·
· Journal of Bacteriology; (United States)
OSTI ID:5864547
- Washington State Univ., Pullman (United States)
Alkaline phosphatase (PhoA) fusions to TonB amino acids 32, 60, 125, 207, 239 (the carboxy terminus) all showed high PhoA activity; a PhoA fusion to TonB amino acid 12 was inactive. The full-length TonB-PhoA fusion protein was associated with the cytoplasmic membrane and retained partial TonB function. These results support a model in which TonB is anchored in the cytoplasmic membrane by its hydrophobic amino terminus, with the remainder of the protein, including its hydrophobic carboxy terminus, extending into the periplasm.
- OSTI ID:
- 5864547
- Journal Information:
- Journal of Bacteriology; (United States), Vol. 173:17; ISSN 0021-9193
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
CELL MEMBRANES
PHYSIOLOGY
ESCHERICHIA COLI
ALKALINE PHOSPHATASE
AMINO ACIDS
BIOPHYSICS
GENES
MEMBRANE TRANSPORT
MOLECULAR STRUCTURE
BACTERIA
CARBOXYLIC ACIDS
CELL CONSTITUENTS
ENZYMES
ESTERASES
HYDROLASES
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHATASES
PROTEINS
551000* - Physiological Systems
550200 - Biochemistry
CELL MEMBRANES
PHYSIOLOGY
ESCHERICHIA COLI
ALKALINE PHOSPHATASE
AMINO ACIDS
BIOPHYSICS
GENES
MEMBRANE TRANSPORT
MOLECULAR STRUCTURE
BACTERIA
CARBOXYLIC ACIDS
CELL CONSTITUENTS
ENZYMES
ESTERASES
HYDROLASES
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHATASES
PROTEINS
551000* - Physiological Systems
550200 - Biochemistry