Natural synthesis of a DNA-binding protein from the C-terminal domain of DNA gyrase A in Borrelia burgdorferi

Scott W. Knight, D. Scott Samuels

Research output: Contribution to journalArticlepeer-review

Abstract

We have identified a 34 kDa DNA-binding protein with an HU-like activity in the Lyme disease spirochete Borrelia burgdorferi. The 34 kDa protein is translated from an abundant transcript initiated within the gene encoding the A subunit of DNA gyrase. Translation of the 34 kDa protein starts at residue 499 of GyrA and proceeds in the same reading frame as full-length GyrA, resulting in an N-terminal-truncated protein. The 34 kDa GyrA C-terminal domain, although not homologous, substitutes for HU in the formation of the Type 1 complex in Mu transposition, and complements an HU-deficient strain of Escherichia coli. This is the first example of constitutive expression of two gene products in the same open reading frame from a single gene in a prokaryotic cellular system.

Original languageEnglish
Pages (from-to)4875-4881
Number of pages7
JournalEMBO Journal
Volume18
Issue number17
DOIs
StatePublished - Sep 1 1999

Keywords

  • Borrelia burgdorferi
  • DNA gyrase
  • HU
  • IHF
  • Mu

Fingerprint

Dive into the research topics of 'Natural synthesis of a DNA-binding protein from the C-terminal domain of DNA gyrase A in Borrelia burgdorferi'. Together they form a unique fingerprint.

Cite this