The ATP-dependent protease Lon (La) of Escherichia coli degrades abnor
mal proteins and is involved in the regulation of capsular polysacchar
ide synthesis. In addition, mutations in the E. coli ion gene suppress
temperature-sensitive mutations in other genes. The ion gene of Borre
lia burgdorferi, encoding a homolog of the Lon protease, has been clon
ed and sequenced. The gene encodes a protein of 806 amino acids. The d
educed amino acid sequence of the B. burgdorferi Lon protease shares s
ubstantial sequence identity with those of other known Lon proteases.
The transcription start point of the B. burgdorferi ion gene was ident
ified 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 ion gene appears to suppress the tempera
ture-sensitive phenotype of an E. coli lpxA mutant. (C) 1997 Elsevier
Science B.V.