NMR spectroscopic investigation of the intecation of single-strand binding protein (SSB) with proteins of the bacterial replication machinery

The information stored in double-stranded DNA is sequestered in the interior of the protective double helix. To provide access to genomic information, dsDNA must be unwound to form single-stranded (ss) intermediates. Since ssDNA is prone to chemical and nucleolytic attacks this process is risky since it can cause damage that is difficult to repair. To help preserve ssDNA intermediates, cells have evolved a specialized class of ssDNA-binding (SSB) proteins that associate with ssDNA with high affinity and in a sequence-independent manner. Beyond their roles in DNA binding, SSB proteins do also associate with a broad array of cellular genome maintenance proteins. This interaction in many cases stimulates the biochemical activities of SSB's partner proteins.
We are using NMR-spectroscopy in conjunction with several labeling pattern to elucidate the interaction of SSB proteins, in particular the C-terminus of SSB proteins, with various interactions partners in the the bacterial replication fork.


N. Naue; M. Beerbaum; A. Bogutzki; P. Schmieder; U. Curth* ; "The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein"; Nucleic Acids Res. 00, 000-000 (2013)

DOI: 10.1093/nar/gkt107

last changes 01.03.2013, Peter Schmieder