(American Society for Microbiology, 2004-12)
Reznikoff, William S.; Bordenstein, Seth R.; Apodaca, Jennifer
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.
