Mechanism of mismatch recognition revealed by human MutSβ bound to unpaired DNA loops
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.2175.pdf
Reference53 articles.
1. Iyer, R.R., Pluciennik, A., Burdett, V. & Modrich, P.L. DNA mismatch repair: functions and mechanisms. Chem. Rev. 106, 302–323 (2006).
2. Junop, M.S., Obmolova, G., Rausch, K., Hsieh, P. & Yang, W. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair. Mol. Cell 7, 1–12 (2001).
3. Habraken, Y., Sung, P., Prakash, L. & Prakash, S. ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2–MSH6 and MLH1–PMS1 protein complexes. J. Biol. Chem. 273, 9837–9841 (1998).
4. Mendillo, M.L. et al. A conserved MutS homolog connector domain interface interacts with MutL homologs. Proc. Natl. Acad. Sci. USA 106, 22223–22228 (2009).
5. Habraken, Y., Sung, P., Prakash, L. & Prakash, S. Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3. Curr. Biol. 6, 1185–1187 (1996).
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