The Lyme Disease Network
Medical / Scientific Abstract


Title:Natural synthesis of a DNA-binding protein from the C-terminal domain of DNA gyrase A in Borrelia burgdorferi.
Authors:Knight SW, Samuels DS
Source:EMBO J 1999 Sep 1;18(17):4875-81
Organization:Division of Biological Sciences, The University of Montana, Missoula, MT 59812, USA.

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.

Keywords:
Amino Acid Sequence, Bacterial Outer Membrane Proteins, METABOLISM, Bacterial Proteins, METABOLISM, Bacteriophage mu, METABOLISM, Base Sequence, Borrelia burgdorferi, GENETICS, METABOLISM, Carrier Proteins, METABOLISM, DNA Topoisomerase (ATP-Hydrolysing), GENETICS, METABOLISM, DNA-Binding Proteins, BIOSYNTHESIS, Gene Expression Regulation, Bacterial, Models, Genetic, Molecular Sequence Data, Nucleoproteins, METABOLISM, RNA, Messenger, ANALYSIS, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Support, Non-U.S. Gov't, Support, U.S. Gov't, Non-P.H.S., Support, U.S. Gov't, P.H.S., Transcription, Genetic

Language: Eng

Unique ID: 99400631


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