In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.

Bacterial ATP-binding cassette (ABC) importers are primary active transporters that are critical for nutrient uptake. Based on structural and functional studies, ABC importers can be divided into two distinct classes, type I and type II. Type I importers follow a strict alternating access mechanism that is driven by the presence of the substrate.

Topology of RbsC, the membrane component of the Escherichia coli ribose transporter.

The topology of RbsC, the membrane component of the ribose transporter in Escherichia coli, has been determined by using 34 single-cysteine mutants and a modified fluorescence labeling technique designated multiplex labeling. This technique gives topology, expression, and localization information for a membrane protein from a single batch of bacterial cells. The results indicate that RbsC contains 10 transmembrane-spanning helices, with the N and C termini being in the cytosol.

Elutability of Proteins from Aluminum-Containing Vaccine Adjuvants by Treatment with Surfactants.

The elutability of proteins from adjuvants in model vaccines composed of ovalbumin adsorbed by aluminum hydroxide adjuvant or lysozyme adsorbed by aluminum phosphate adjuvant following treatment with surfactant solutions was studied. Nonionic (Triton X-100, lauryl maltoside), zwitterionic (lauryl sulfobetaine), anionic (sodium dodecyl sulfate), and cationic (cetylpyridinium chloride, dodecyltrimethylammonium chloride) surfactants were investigated. Cetylpyridinium chloride produced the greatest degree of elution (60%) of ovalbumin from aluminum hydroxide adjuvant.

The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC.

Chimeric genes encoding full-length copies of rbsA and rbsC connected by segments coding for short bridge peptides were constructed and expressed in Escherichia coli. Surprisingly, the chimeric genes complemented the strain in which rbsA and rbsC were deleted. The chimeric proteins were overproduced, and the products were purified by affinity chromatography.