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), Journal Name: Journal of Bacteriology; (United States) Vol. 173:17; ISSN JOBAA; ISSN 0021-9193
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550200 -- Biochemistry
551000* -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ALKALINE PHOSPHATASE
AMINO ACIDS
BACTERIA
BIOPHYSICS
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CELL MEMBRANES
ENZYMES
ESCHERICHIA COLI
ESTERASES
GENES
HYDROLASES
MEMBRANE TRANSPORT
MEMBRANES
MICROORGANISMS
MOLECULAR STRUCTURE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHATASES
PHYSIOLOGY
PROTEINS
551000* -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ALKALINE PHOSPHATASE
AMINO ACIDS
BACTERIA
BIOPHYSICS
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CELL MEMBRANES
ENZYMES
ESCHERICHIA COLI
ESTERASES
GENES
HYDROLASES
MEMBRANE TRANSPORT
MEMBRANES
MICROORGANISMS
MOLECULAR STRUCTURE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHATASES
PHYSIOLOGY
PROTEINS