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Recent Article: Structure Activity Relationships Reveal Key Features of 8-Oxoguanine:A Mismatch Detection by the MutY Glycosylase
MutY, remarkably, is able to specifically recognize and initiate repair of target OG:A mismatches from among a vast sea of natural DNA. To help reveal molecular features of OG that are critical for MutY recognition, this work explored the effects of systematic OG:A substrate alterations on MutY recognition in a cellular context. OG analogs were synthesized, assembled into OG:A modified oligonucleotides, and were subsequently analyzed using binding, enzymatic, and cellular repair assays. Click to find out more!
Recent Article: S K-edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY
In this work, the iron-sulfur clusters of DNA repair glycosylases Endonuclease III and MutY were examined using S K-edge X-ray Absorption Spectroscopy (XAS) in order to investigate DNA binding and solvation effects on Fe-S bond covalencies. Results were compared to data obtained from previously studied model complexes such as ferredoxin (Fd) and high potential iron-sulfur protein (HiPiP). Click to read more about changes in Fe-S bond covalency using EndoIII and MutY protein models.
Recent Article: Repair of 8-OXOG:A Mismatches by the MUTYH Glycosylase: Mechanisms, Metals and Medicine
This in-depth review examines the role MUTYH structure and related function play in the development of human disease such as MUTYH-Associated Polyposis (MAP). Additionally, the importance of MUTYH’s metal cofactor sites is discussed, and recent updates to the catalytic mechanism are provided. Also, insight obtained from MAP-associated MUTYH variant studies is discussed, and the dynamic nature of MUTYH is explored. Click to read the article and find out more.