The University of Tokyo · Biochemistry, Genetics and Molecular Biology
Professor Hiroyuki Aburatani's research lab focuses on DNA damage and repair mechanisms, particularly the enzymatic pathways involved in recognizing and repairing oxidative DNA lesions such as 8-hydroxyguanine (8-OH-G). The lab investigates the molecular functions of DNA glycosylases, including the human homolog of the yeast OGG1 protein (hMMH), which plays a key role in base excision repair. Their work bridges molecular biology and cancer research, aiming to understand how endogenous oxidative stress contributes to mutagenesis and aging-related diseases. The lab also explores the genetic and structural basis of DNA repair enzymes using bioinformatics and molecular cloning techniques.
Figures are computed from collected data and may differ slightly.
8-Hydroxyguanine (8-OH-G) is one of the major DNA oxidation products implicated in mutagenesis induced by oxygen radical-forming agents, including ionizing radiation. It is also believed to be involved in spontaneous mutation induced by metabolically produced oxygen radicals. A mammalian homologue of 8-OH-G glycosylase/apurinic, apyrimidinic lyase (mutM homologue, MMH) has been identified in the EST database (for expressed sequence tags) through a homology search with yeast OGG1 protein. The hum
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