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Journal of Bacteriology, December 2004, p. 8240-8247, Vol. 186, No. 24
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.24.8240-8247.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Josephine Bay Paul Center for Comparative Molecular Biology and Evolution, Marine Biological Laboratory, Woods Hole, Massachusetts,1 Department of Biochemistry, University of Wisconsin, Madison, Wisconsin2
Received 14 May 2004/ Accepted 10 September 2004
Comparative sequence analysis of IS50 transposase-related protein sequences in conjunction with known structural, biochemical, and genetic data was used to determine domains and residues that play key roles in IS50 transposase function. BLAST and ClustalW analyses have been used to find and analyze six complete protein sequences that are related to the IS50 transposase. The protein sequence identity of these six homologs ranged from 25 to 55% in comparison to the IS50 transposase. Homologous motifs were found associated with each of the three catalytic residues. Residues that play roles in transposase-DNA binding, protein autoregulation, and DNA hairpin formation were also found to be conserved in addition to other residues of unknown function. On the other hand, some homologous sequences did not appear to be competent to encode the inhibitor regulatory protein. The results were also used to compare the IS50 transposase with the more distantly related transposase encoded by IS10.
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