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Natural synthesis of a DNA‐binding protein from the C‐terminal domain of DNA gyrase A in Borrelia burgdorferi
Author(s) -
Knight Scott W.,
Samuels D.Scott
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.17.4875
Subject(s) - knight , borrelia burgdorferi , biology , library science , dna , genetics , physics , computer science , antibody , astronomy
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.