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Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.


ABSTRACT: A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between the S. aureus and B. burgdorferi proteins identified that a 6-residue stretch of the SpoVG ?-helix contributes to DNA sequence specificity. Two additional, highly conserved amino acid residues on an adjacent ?-sheet are essential for DNA-binding, apparently by contacts with the DNA phosphate backbone. Results of these studies thus identified a novel family of bacterial DNA-binding proteins, developed a model of SpoVG-DNA interactions, and provide direction for future functional studies on these wide-spread proteins.

SUBMITTER: Jutras BL 

PROVIDER: S-EPMC3688583 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Eubacterial SpoVG homologs constitute a new family of site-specific DNA-binding proteins.

Jutras Brandon L BL   Chenail Alicia M AM   Rowland Christi L CL   Carroll Dustin D   Miller M Clarke MC   Bykowski Tomasz T   Stevenson Brian B  

PloS one 20130620 6


A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between t  ...[more]

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