Cloning and expression of the Borrelia burgdorferi lon gene

Joann L. Cloud, Richard T. Marconi, Christian H. Eggers, Claude F. Garon, Kit Tilly, D. Scott Samuels

Research output: Contribution to journalArticlepeer-review

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. colil The 5'-end of the B. burgdorferi lon gene appears to suppress the temperature-sensitive phenotype of an E. coli lpxA mutant.

Original languageEnglish
Pages (from-to)137-141
Number of pages5
JournalGene
Volume194
Issue number1
DOIs
StatePublished - Jul 18 1997

Keywords

  • ATP-dependent protease
  • Lyme disease
  • Temperature-sensitive mutant
  • lpxA

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