Mutations in the Conserved Glycine and Serine of the MutS ABC signature motif affect Nucleotide Exchange, Kinetics of sliding clamp release of mismatch and mismatch repair

Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis

Volumn 684, Issue 1-2, 2010, Pages 56-65

  Acharya, Samir ^a   Patterson, Kara ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

ABC transporters; Mismatch repair; MutS; MutS clamp; Nucleotide exchange; Signature motif

Indexed keywords

ABC TRANSPORTER; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLYCINE; PROTEIN MUTS; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENETICS; BASE MISPAIRING; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION; DNA REPAIR; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENE MUTATION; GENETIC CONSERVATION; GENETIC STABILITY; HYDROLYSIS; IN VIVO STUDY; MISMATCH REPAIR; MOLECULAR RECOGNITION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ATP-BINDING CASSETTE TRANSPORTERS; DNA MISMATCH REPAIR; ESCHERICHIA COLI PROTEINS; GLYCINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; MUTS DNA MISMATCH-BINDING PROTEIN; NUCLEOTIDES; SERINE;

ESCHERICHIA COLI;

EID: 73949121668     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2009.11.007     Document Type: Article

References (39)

1. Acharya S. Mutations in the signature motif in MutS affect ATP-induced clamp formation and mismatch repair. Mol. Microbiol. 69 (2008) 1544-1559
2. Friedberg E.C., Walker G.C., and Siede W. DNA Repair and Mutagenesis (2005), American Society for Microbiology, Washington, D.C.
3. Fishel R., and Wilson T. MutS homologs in mammalian cells. Curr. Opin. Genet. Dev. 7 (1997) 105-113
4. Kolodner R.D., and Marsischky G.T. Eukaryotic DNA mismatch repair. Curr. Opin. Genet. Dev. 9 (1999) 89-96
5. Kunkel T.A., and Erie D.A. DNA Mismatch Repair. Annu. Rev. Biochem. 74 (2005) 681-710
6. Jiricny J. The multifaceted mismatch-repair system. Nat. Rev. Mol. Cell Biol. 7 (2006) 335-346
7. Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 (1982) 945-951
8. Lamers M.H., Perrakis A., Enzlin J.H., Winterwerp H.H., de Wind N., and Sixma T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G × T mismatch. Nature 407 (2000) 711-717
9. Obmolova G., Ban C., Hsieh P., and Yang W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407 (2000) 703-710
10. Hsieh P., and Yamane K. DNA mismatch repair: molecular mechanism, cancer, and ageing. DNA Repair 129 (2008) 391-407
11. Allen D.J., Makhov A., Grilley M., Taylor J., Thresher R., Modrich P., and Griffith J.D. MutS mediates heteroduplex loop formation by a translocation mechanism. EMBO J. 16 (1997) 4467-4476
12. 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
13. 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
14. Blackwell L.J., Bjornson K.P., Allen D.J., and Modrich P. Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis. J. Biol. Chem. 276 (2001) 34339-34347
15. 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
16. 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
17. Mazur D.J., Mendillo M.L., and Kolodner R.D. Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA. Mol. Cell 22 (2006) 39-49
18. Gorman J., Chowdhury A., Surtees J.A., Shimada J., Reichman D.R., Alani E., and Greene E.C. Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6. Mol. Cell 28 (2007) 359
19. Dufner P., Marra G., Raschle M., and Jiricny J. Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit. J. Biol. Chem. 275 (2000) 36550-36555
20. Drotschmann K., Yang W., Brownewell F.E., Kool E.T., and Kunkel T.A. Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. J. Biol. Chem. 276 (2001) 46225-46229
21. Drotschmann K., Yang W., and Kunkel T.A. Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6. DNA Repair 1 (2002) 743-753
22. Bjornson K.P., and Modrich P. Differential and simultaneous adenosine di- and triphosphate binding by MutS. J. Biol. Chem. 278 (2003) 18557-18562
23. Lamers M.H., Winterwerp H.H., and Sixma T.K. The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J. 22 (2003) 746-756
24. 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
25. Martik D., Baitinger C., and Modrich P. Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites. J. Biol. Chem. 279 (2004) 28402-28410
26. Gradia S., Acharya S., and Fishel R. The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch. J. Biol. Chem. 275 (2000) 3922-3930
27. 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 domains. Implications for ATP hydrolysis and conformational changes. J. Biol. Chem. 279 (2004) 43879-43885
28. Hopfner K.-P., and Tainer J.A. Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Curr. Opin. Struct. Biol. 13 (2003) 249-255
29. Moncalian G., Lengsfeld B., Bhaskara V., Hopfner K.-P., Karcher A., Alden E., Tainer J.A., and Paull T.T. The Rad50 signature motif: essential to ATP binding and biological function. J. Mol. Biol. 335 (2004) 937
30. Davidson A.L., and Maloney P.C. ABC transporters: how small machines do a big job. Trends Microbiol. 15 (2007) 448
31. Tombline G., and Senior A.E. The occluded nucleotide conformation of P-glycoprotein. J. Bioenerg. Biomem. 37 (2005) 497-500
32. Tombline G., Muharemagic A., White L.B., and Senior A.E. Involvement of the "occluded nucleotide conformation" of P-glycoprotein in the catalytic pathway. Biochemistry 44 (2005) 12879-12886
33. Lebbink J.H., Georgijevic D., Natrajan G., Fish A., Winterwerp H.H., Sixma T.K., and de Wind N. Dual role of MutS glutamate 38 in DNA mismatch discrimination and in the authorization of repair. EMBO J. 25 (2006) 409-419
34. Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C., and Fishel R. HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions. Cancer Cell 1 (2002) 469-478
35. Cyr J.L., and Heinen C.D. Hereditary cancer-associated missense mutations in hMSH6 uncouple ATP hydrolysis from DNA mismatch binding. J. Biol. Chem. 283 (2008) 31641-31648
36. Hess M.T., Gupta R.D., and Kolodner R.D. Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP. J. Biol. Chem. 277 (2002) 25545-25553
37. Haber L.T., and Walker G.C. Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities. EMBO J. 10 (1991) 2707-2715
38. Ollila S., Bebek D.D., Jiricny J., and Nystrom M. Mechanisms of pathogenicity in human MSH2 missense mutants. Hum. Mut. 29 (2008) 1355-1363
39. Lutzen A., de Wind N., Georgijevic D., Nielsen F.C., and Rasmussen L.J. Functional analysis of HNPCC-related missense mutations in MSH2. Mut. Res. 645 (2008) 44-55