Presenter Information

Mason ConenFollow

Presentation Type

Poster

Abstract

Cr(V) is a carcinogen that oxidizes guanine aggressively to form spiroiminodihydantion (Sp) and guanidinohydantoin (Gh), both of which cause G→T transversion mutations at a high rate and contain unusual hydantoin moieties. Endonuclease VIII (nei) can recognize and excise these oxidation products from DNA and is translated as one of five protein products of the Nei operon in Escherichia coli (E. coli). However, the functions of the other four proteins remain unknown. To address this gap in knowledge, we focused on one of the four that immediately precedes nei, the ybgL protein. Previous work by our group has suggested a role for ybgL in vitro. In the current study, we attempt to characterize the role of ybgL by oxidizing a synthetic oligo with Cr(V) and reacting the oxidized oligo with ybgL in the presence of different potential cofactors. Due to the presence of hydantoin moieties within the DNA, we will model the ybgL protein to the Hydantoinase B class of enzymes, which recognize the hydantoin moiety. This study will attempt to elucidate the role of an uncharacterized protein in excising oxidation lesions caused by chromium toxicity.

Category

Life Sciences

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Apr 28th, 3:00 PM Apr 28th, 4:00 PM

The E. coli Protein YbgL: A Novel DNA Repair Enzyme?

UC South Ballroom

Cr(V) is a carcinogen that oxidizes guanine aggressively to form spiroiminodihydantion (Sp) and guanidinohydantoin (Gh), both of which cause G→T transversion mutations at a high rate and contain unusual hydantoin moieties. Endonuclease VIII (nei) can recognize and excise these oxidation products from DNA and is translated as one of five protein products of the Nei operon in Escherichia coli (E. coli). However, the functions of the other four proteins remain unknown. To address this gap in knowledge, we focused on one of the four that immediately precedes nei, the ybgL protein. Previous work by our group has suggested a role for ybgL in vitro. In the current study, we attempt to characterize the role of ybgL by oxidizing a synthetic oligo with Cr(V) and reacting the oxidized oligo with ybgL in the presence of different potential cofactors. Due to the presence of hydantoin moieties within the DNA, we will model the ybgL protein to the Hydantoinase B class of enzymes, which recognize the hydantoin moiety. This study will attempt to elucidate the role of an uncharacterized protein in excising oxidation lesions caused by chromium toxicity.