The Chlamydia trachomatis hyp operon is homologous to the groE stress response operon of Escherichia coli.
The Chlamydia trachomatis serovar A hyp operon was cloned, sequenced, and expressed in Escherichia coli. Two cotranscribed open reading frames, hypA and hypB, encoded polypeptides of 17 and 57 kilodaltons, respectively. The deduced amino acid sequences of serovar A HypA and HypB proteins were (respectively) 85 and 94% identical with HypA and HypB proteins of Chlamydia psittaci GPIC, and HypB was greater than 50% identical to 60-kilodalton stress response proteins from other procaryotes and eucaryotes. The sequence should be useful in defining the antigenic structure of the Chlamydia trachomatis HypB protein, a necessary step toward understanding the relationship between the immune response to this protein and the pathogenesis of human chlamydial diseases.
Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840.
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Morrison
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D002692:Chlamydia trachomatis / Q000145:classification / Q000235:genetics*; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000145:classification / Q000235:genetics*; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D009876:Operon; D011993:Recombinant Fusion Proteins / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D011993:Recombinant Fusion Proteins