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The global regulator H‐NS binds to two distinct classes of sites within the Tn10 transpososome to promote transposition
Author(s) -
Ward Chris M.,
Wardle Simon J.,
Singh Randeep K.,
Haniford David B.
Publication year - 2007
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2007.05708.x
Subject(s) - tn10 , transposase , biology , transposable element , tn3 transposon , transposition (logic) , p element , microbiology and biotechnology , dna , bacteriophage mu , genetics , mutant , gene , linguistics , philosophy
Summary 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.