Identification of critical residues required for the mutation avoidance function of human MutY (hMYH) and implications in colorectal cancer

Steven H. Wooden, Heather M. Bassett, Thomas Wood, Amanda K. McCullough

Research output: Contribution to journalArticle

33 Scopus citations


Mutations found in human tumors often include transversions of GC to TA that may result from the mis-pairing of 8-oxoG with adenine during DNA replication. The human MutY (hMYH) enzyme, an adenine-specific DNA glycosylase, initiates repair at this mismatch. It has recently been demonstrated that inherited variants of hMYH may predispose individuals to multiple colorectal adenomas and carcinoma [Nat. Genet. 30 (2002) 227]. In this study, we demonstrate that two of these cancer-associated hMYH mutants, Y165C and G382D, are devoid of glycosylase activity directed towards 8-oxoG:A mispairs. These findings implicate a total loss of hMYH function associated with colorectal cancers.

Original languageEnglish (US)
Pages (from-to)89-95
Number of pages7
JournalCancer Letters
Issue number1
StatePublished - Mar 8 2004



  • Cancer
  • Colorectal adenomas
  • DNA repair
  • MutY
  • Oxidative damage

ASJC Scopus subject areas

  • Cancer Research
  • Molecular Biology
  • Oncology

Cite this