Characterization of a stress protein from group B Neisseria meningitidis.
Increased levels of a 65-kDa stress protein (Msp65) were observed in group B Neisseria meningitidis grown under stationary-growth conditions. Electron microscopy showed two apposing rings of seven subunits, a structure typical of Escherichia coli GroEL. Msp65 was not found in either the periplasmic space or the outer membrane. Several important differences between the GroEL analogs of N. meningitidis and Neisseria gonorrhoeae are discussed.
Arakere
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Division of Bacterial Products, Food and Drug Administration, Bethesda, Maryland 20892.
Kessel
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M
Nguyen
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N
Frasch
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CE
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D018834:Chaperonin 60; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009344:Neisseria gonorrhoeae / Q000737:chemistry; D009345:Neisseria meningitidis / Q000737:chemistry*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins