Effect of E. coli MutL on the steady-state ATPase activity of MutS in the presence of short blocked end DNAs.
The effect of wild-type and mutant MutL on the steady-state ATPase activity of MutS from Escherichia coli has been investigated in the absence and presence of 22, 50, and 75 base pair hetero- and homoduplex DNAs with open and blocked ends. The steady-state ATPase activity of MutS has been measured at 37 degrees C using a spectrophotometric method. The presence of MutL did not affect appreciably on the ATPase activity of MutS in the absence of DNA or in the presence of blocked end homoduplex DNAs. However, the addition of MutL affected oppositely on the ATPase activity of MutS in the presence of G-T mismatched DNAs depending on their end status. We have also found that only the ATPase active forms of MutL increased the ATPase activity of MutS in the presence of G-T mismatched DNAs with blocked ends. The results suggest that MutL ATPase activity is required to catalyze dissociation of the MutS sliding clamps.
Heo
Seong-Dal
SD
Department of Chemistry, Pohang University of Science and Technology, Pohang, Gyeongbuk, Republic of Korea.
Ku
Ja Kang
JK
Ban
Changill
C
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D004247:DNA / Q000235:genetics / Q000378:metabolism*; D053843:DNA Mismatch Repair; D004261:DNA Replication; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D000070956:MutL Proteins; D051719:MutS DNA Mismatch-Binding Protein / Q000378:metabolism*
D029968:Escherichia coli Proteins; C074770:MutL protein, E coli; D004247:DNA; D000251:Adenosine Triphosphatases; D000070956:MutL Proteins; D051719:MutS DNA Mismatch-Binding Protein; C497175:MutS protein, E coli