1. Cloning and expression of the Borrelia burgdorferi lon gene.
- Author
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Cloud JL, Marconi RT, Eggers CH, Garon CF, Tilly K, and Samuels DS
- Subjects
- ATP-Dependent Proteases, Adenosine Triphosphatases biosynthesis, Adenosine Triphosphatases genetics, Amino Acid Sequence, Base Sequence, Cloning, Molecular, Escherichia coli enzymology, Genetic Complementation Test, Heat-Shock Proteins biosynthesis, Heat-Shock Proteins chemistry, Molecular Sequence Data, Phylogeny, Polysaccharides, Bacterial biosynthesis, Promoter Regions, Genetic, Recombinant Proteins biosynthesis, Sequence Alignment, Sequence Homology, Amino Acid, Serine Endopeptidases biosynthesis, Serine Endopeptidases chemistry, Transcription, Genetic, Borrelia burgdorferi Group enzymology, Borrelia burgdorferi Group genetics, Escherichia coli Proteins, Heat-Shock Proteins genetics, Protease La, Serine Endopeptidases genetics
- Abstract
The ATP-dependent protease Lon (La) of Escherichia coli degrades abnormal proteins and is involved in the regulation of capsular polysaccharide synthesis. In addition, mutations in the E. coli lon gene suppress temperature-sensitive mutations in other genes. The lon gene of Borrelia burgdorferi, encoding a homolog of the Lon protease, has been cloned and sequenced. The gene encodes a protein of 806 amino acids. The deduced amino acid sequence of the B. burgdorferi Lon protease shares substantial sequence identity with those of other known Lon proteases. The transcription start point of the B. burgdorferi lon gene was identified by primer extension analysis and the potential promoter did not show similarities to the consensus heat-shock promoter in E. coli. The 5'-end of the B. burgdorferi lon gene appears to suppress the temperature-sensitive phenotype of an E. coli lpxA mutant.
- Published
- 1997
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