The tale of SSB

Research output: Contribution to journalReview articlepeer-review

32 Scopus citations

Abstract

The E. coli single stranded DNA binding protein (SSB) is essential to all aspects of DNA metabolism. Here, it has two seemingly disparate but equally important roles: it binds rapidly and cooperatively to single stranded DNA (ssDNA) and it binds to partner proteins that constitute the SSB interactome. These two roles are not disparate but are instead, intimately linked. A model is presented wherein the intrinsically disordered linker (IDL) is directly responsible for mediating protein-protein interactions. It does this by binding, via PXXP motifs, to the OB-fold (aka SH3 domain) of a nearby protein. When the nearby protein is another SSB tetramer, this leads to a highly efficient ssDNA binding reaction that rapidly and cooperatively covers and protects the exposed nucleic acid from degradation. Alternatively, when the nearby protein is a member of the SSB interactome, loading of the enzyme onto the DNA takes places.

Original languageEnglish (US)
Pages (from-to)111-118
Number of pages8
JournalProgress in Biophysics and Molecular Biology
Volume127
DOIs
StatePublished - Aug 2017
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Molecular Biology

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