Effect of E. coli MutL on the steady-state ATPase activity of MutS in the presence of short blocked end DNAs

Biochemical and Biophysical Research Communications

Volumn 385, Issue 2, 2009, Pages 225-229

  Heo, Seong Dal ^a   Ku, Ja Kang ^a   Ban, Changill ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

ATPase activity; Blocked heteroduplex DNA; MMR mechanism; MutL; MutS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL DNA; DOUBLE STRANDED DNA; GUANOSINE; HETERODUPLEX; MUTANT PROTEIN; PROTEIN MUTL; PROTEIN MUTS; TYROSINE;

ARTICLE; BASE MISPAIRING; CATALYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; SPECTROPHOTOMETRY; STEADY STATE; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; CATALYSIS; DNA; DNA MISMATCH REPAIR; DNA REPLICATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MUTS DNA MISMATCH-BINDING PROTEIN;

ESCHERICHIA COLI;

EID: 67349149025     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.05.042     Document Type: Article

References (25)

1. Iyer R.R., Pluciennik A., Burdett V., and Modrich P. DNA mismatch repair: functions and mechanisms. Chem. Rev. 106 (2006) 302-323
2. Hsieh P., and Yamane K. DNA mismatch repair: molecular mechanism, cancer, and ageing. Mech. Ageing Dev. 129 (2008) 391-407
3. Blackwell L.J., Wang S., and Modrich P. DNA chain length dependence of formation and dynamics of hMutSα·hMutLα·Hheteroduplex complexes. J. Biol. Chem. 276 (2001) 33233-33240
4. Schofield M.J., Nayak S., Scott T.H., Du C., and Hsieh P. Interaction of Escherichia coli MutS and MutL at a DNA mismatch. J. Biol. Chem. 276 (2001) 28291-28299
5. Acharya S., Foster P.L., Brooks P., and Fishel R. The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair. Mol. Cell 12 (2003) 233-246
6. Selmane T., Schofield M.J., Nayak S., Du C., and Hsieh P. Formation of a DNA mismatch repair complex mediated by ATP. J. Mol. Biol. 334 (2003) 949-956
7. Hall M.C., and Matson S.W. The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity. J. Biol. Chem. 274 (1999) 1306-1312
8. Junop M.S., Yang W., Funchain P., Clendenin W., and Miller J.H. In vitro and in vivo studies of MutS, MutL, and MutH mutants: correlation of mismatch repair and DNA recombination. DNA Repair 2 (2003) 387-405
9. Mechanic L.E., Frankel B.A., and Matson S.W. Escherichia coli MutL loads DNA helicase II onto DNA. J. Biol. Chem. 275 (2000) 38337-38346
10. Guarne A., Ramon-Maiques S., Wolff E.M., Ghirlando R., Hu X., Miller J.H., and Yang W. Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair. EMBO J. 23 (2004) 4134-4145
11. Robertson A.B., Pattishall S.A., Gibbons E.A., and Matson S.W. MutL-catalyzed ATP hydrolysis is required at a post-Uvrd loading step in methyl-directed mismatch repair. J. Biol. Chem. 281 (2006) 19949-19959
12. Lamers M.H., Winterwerp H.H.K., and Sixma T.K. The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J. 22 (2003) 746-756
13. Antony E., and Hingorani M.M. Asymmetric ATP binding and hydrolysis activity of the thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. Biochemistry 43 (2004) 13115-13128
14. Bjornson K.P., Allen D.J., and Modrich P. Modulation of MutS ATP hydrolysis by DNA cofactors. Biochemistry 39 (2000) 3176-3183
15. Antony E., and Hingorani M.M. Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair. Biochemistry 42 (2003) 7682-7693
16. Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J., and Fishel R. HMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA. Mol. Cell 3 (1999) 255-261
17. Gradia S., Acharya S., and Fishel R. The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch. Cell 91 (1997) 995-1005
18. Joseph N., Sawarkar R., and Rao D.N. DNA mismatch correction in haemophilus influenzae: characterization of MutL, MutH and their interaction. DNA Repair 3 (2004) 1561-1577
19. Heo S.D., Cho M., Ku J.K., and Ban C. Steady-state ATPase activity of E. coli MutS modulated by its dissociation from heteroduplex DNA. Biochem. Biophys. Res. Commun. 364 (2007) 264-269
20. Ban C., Junop M., and Yang W. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97 (1999) 85-97
21. Spampinato C., and Modrich P. The MutL ATPase is required for mismatch repair. J. Biol. Chem. 275 (2000) 9863-9869
22. Takashi R., and Putnam S. A fluorimetric method for continuously assaying ATPase: application to small specimens of glycerol-extracted muscle fibers. Anal. Biochem. 92 (1979) 375-382
23. Niemeyer C.M., Adler M., Pignataro B., Lenhert S., Gao S., Chi L., Fuchs H., and Blohm D. Self-assembly of DNA streptavidin nanostructures and their use as reagents in immuno-PCR. Nucleic Acids Res. 27 (1999) 4553-4561
24. Kolodner R.D., Mendillo M.L., and Putnam C.D. Coupling distant sites in DNA during DNA mismatch repair. Proc. Natl. Acad. Sci. USA 104 (2007) 12953-12954
25. Lamers M.H., Georgijevic D., Lebbink J.H., Winterwerp H.H.K., Agianian B., de Wind N., and Sixma T.K. ATP increases the affinity between MutS ATPase domain. J. Biol. Chem. 279 (2004) 43879-43885