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- Title
The global regulator H-NS binds to two distinct classes of sites within the Tn10 transpososome to promote transposition.
- Authors
Ward, Chris M.; Wardle, Simon J.; Singh, Randeep K.; Haniford, David B.
- Abstract
The histone-like nucleoid structuring protein (H-NS) is a global transcriptional regulator that influences stress response and virulence pathways in Gram-negative bacteria. H-NS also promotes Tn10 transposition by binding directly to the transpososome and inducing a conformational change in the transpososome that favours intermolecular transposition events. H-NS binds preferentially to curved DNA and can bend non-curved DNA, it self-oligomerizes and can interact with other proteins. To determine what functions of H-NS are important in promoting Tn10 transposition, we have examined the ability of two mutant forms of H-NS, P116S and 1–64, to act in Tn10 transposition. We provide evidence that the initial interaction of H-NS with the transpososome is dependent on H-NS binding to a specific structure in DNA flanking the transposon end. Additional molecules of H-NS then bind within the transposon end. This latter event appears to be directed by H-NS binding to the Tn10 transposase protein, and is important in maintaining the transpososome in a conformation that promotes intermolecular transposition. The binding of H-NS to a transposase protein is a novel function for this important regulatory molecule.
- Subjects
HISTONES; NUCLEOIDS; GRAM-negative bacteria; DNA; PROTEIN binding; TRANSPOSONS
- Publication
Molecular Microbiology, 2007, Vol 64, Issue 4, p1000
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.2007.05708.x