1l2b Citations

Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.

Nat Struct Biol 9 544-52 (2002)
Related entries: 1l1t, 1l1z, 1l2c, 1l2d

Cited: 101 times
EuropePMC logo PMID: 12055620

Abstract

MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating base-excision repair of oxidized guanine residues in DNA. Here we report five different crystal structures of MutM-DNA complexes that represent different steps of the repair reaction cascade catalyzed by the protein and also differ in the identity of the base opposite the lesion (the 'estranged' base). These structures reveal that the MutM active site performs the multiple steps of base-excision and 3' and 5' nicking with minimal rearrangement of the DNA backbone.

Reviews - 1l2b mentioned but not cited (2)

  1. Recent advances in the structural mechanisms of DNA glycosylases. Brooks SC, Adhikary S, Rubinson EH, Eichman BF. Biochim Biophys Acta 1834 247-271 (2013)
  2. The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage. Prakash A, Doublié S, Wallace SS. Prog Mol Biol Transl Sci 110 71-91 (2012)

Articles - 1l2b mentioned but not cited (1)



Reviews citing this publication (19)

  1. DNA base damage recognition and removal: new twists and grooves. Huffman JL, Sundheim O, Tainer JA. Mutat Res 577 55-76 (2005)
  2. DNA glycosylase recognition and catalysis. Fromme JC, Banerjee A, Banerjee A, Verdine GL. Curr Opin Struct Biol 14 43-49 (2004)
  3. Structural characterization of the Fpg family of DNA glycosylases. Zharkov DO, Shoham G, Grollman AP. DNA Repair (Amst) 2 839-862 (2003)
  4. DNA base repair--recognition and initiation of catalysis. Dalhus B, Laerdahl JK, Backe PH, Bjørås M. FEMS Microbiol Rev 33 1044-1078 (2009)
  5. Covalent trapping of protein-DNA complexes. Verdine GL, Norman DP. Annu Rev Biochem 72 337-366 (2003)
  6. Repair of 8-oxo-7,8-dihydroguanine in prokaryotic and eukaryotic cells: Properties and biological roles of the Fpg and OGG1 DNA N-glycosylases. Boiteux S, Coste F, Castaing B. Free Radic Biol Med 107 179-201 (2017)
  7. Base excision repair and its role in maintaining genome stability. Baute J, Depicker A. Crit Rev Biochem Mol Biol 43 239-276 (2008)
  8. Biological properties of single chemical-DNA adducts: a twenty year perspective. Delaney JC, Essigmann JM. Chem Res Toxicol 21 232-252 (2008)
  9. DNA glycosylases search for and remove oxidized DNA bases. Wallace SS. Environ Mol Mutagen 54 691-704 (2013)
  10. The DNA trackwalkers: principles of lesion search and recognition by DNA glycosylases. Zharkov DO, Grollman AP. Mutat Res 577 24-54 (2005)
  11. Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine. Banda DM, Nuñez NN, Burnside MA, Bradshaw KM, David SS. Free Radic Biol Med 107 202-215 (2017)
  12. The formamidopyrimidines: purine lesions formed in competition with 8-oxopurines from oxidative stress. Greenberg MM. Acc Chem Res 45 588-597 (2012)
  13. Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage. Liu M, Doublié S, Wallace SS. Mutat Res 743-744 4-11 (2013)
  14. Repair of oxidatively induced DNA damage by DNA glycosylases: Mechanisms of action, substrate specificities and excision kinetics. Dizdaroglu M, Coskun E, Jaruga P. Mutat Res Rev Mutat Res 771 99-127 (2017)
  15. Regulation of DNA glycosylases and their role in limiting disease. Sampath H, McCullough AK, Lloyd RS. Free Radic Res 46 460-478 (2012)
  16. Incomplete base excision repair contributes to cell death from antibiotics and other stresses. Gruber CC, Walker GC. DNA Repair (Amst) 71 108-117 (2018)
  17. Bacterial DNA excision repair pathways. Wozniak KJ, Simmons LA. Nat Rev Microbiol 20 465-477 (2022)
  18. DNA repair: how MutM finds the needle in a haystack. Jiricny J. Curr Biol 20 R145-7 (2010)
  19. Main factors providing specificity of repair enzymes. Nevinsky GA. Biochemistry (Mosc) 76 94-117 (2011)

Articles citing this publication (79)