TY - JOUR
T1 - Comparative sequence analysis of IS50/Tn5 transposase
AU - Reznikoff, William S.
AU - Bordenstein, Seth R.
AU - Apodaca, Jennifer
PY - 2004/12
Y1 - 2004/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=10044293093&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=10044293093&partnerID=8YFLogxK
U2 - 10.1128/JB.186.24.8240-8247.2004
DO - 10.1128/JB.186.24.8240-8247.2004
M3 - Article
C2 - 15576772
AN - SCOPUS:10044293093
SN - 0021-9193
VL - 186
SP - 8240
EP - 8247
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 24
ER -