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Papers In Press, published online ahead of print December 27, 2001
J. Biol. Chem, 10.1074/jbc.M110341200
Submitted on October 26, 2001
Revised on December 25, 2001
Accepted on December 26, 2001
Biology, Massachusetts Institute of Technology, Cambridge, MA 02139
Corresponding Author: ilana{at}mit.edu
Mu transposition occurs within a large protein-DNA complex called a transpososome. This stable complex includes four subunits of MuA transposase, each contacting a 22 base-pair recognition site located near an end of the transposon DNA. These MuA recognition sites are critical for assembling the transpososome. Here we report that when concentrations of Mu DNA are limited, the MuA recognition sites permit assembly of transpososomes in which non-Mu DNA substitutes for some of the Mu sequences. These "hybrid" transpososomes are stable to competitor DNA, actively transpose the non-Mu DNA, and produce transposition products which had been previously observed but not explained. The strongest activator of non-Mu transposition is a DNA fragment containing two MuA recognition sites and no cleavage site, but a shorter fragment with just one recognition site is sufficient. Based on our results, we propose that MuA recognition sites drive assembly of functional transpososomes in two complementary ways. Multiple recognition sites help physically position MuA subunits in the transpososome, plus each individual site allosterically activates transposase.
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