Date of Presentation

5-6-2021 12:00 AM

College

School of Osteopathic Medicine

Poster Abstract

Replication Protein A (RPA) is a single stranded DNA binding protein which stabilizes ssDNA for replication and repair. One function of RPA is to bind the DNA repair enzyme uracil DNA glycosylase (UNG2) and direct its activity towards ssDNA dsDNA junctions.

UNG2 removes uracil bases from DNA which can appear through dUMP misincorporation or through cytosine deamination. If uracil is present instead of a cytosine, then the original GC pair becomes a GU pair. The uracil will then base pair to adenine in the replicated daughter strand. This results in a GC → AT mutation that could contribute to cancer formation.

RPA is known to target UNG2 towards individual uracil bases. We hypothesize that RPA will target UNG2 to uracil bases in DNA regardless of the number of uracils in the DNA strand.

Keywords

Uracil, Replication Protein A, DNA, Mutation

Disciplines

Genetic Processes | Medical Molecular Biology | Medicine and Health Sciences | Molecular Biology | Neoplasms

Document Type

Poster

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May 6th, 12:00 AM

Replication Protein A (RPA) Targeting of Uracil DNA Glycosylase (UNG2)

Replication Protein A (RPA) is a single stranded DNA binding protein which stabilizes ssDNA for replication and repair. One function of RPA is to bind the DNA repair enzyme uracil DNA glycosylase (UNG2) and direct its activity towards ssDNA dsDNA junctions.

UNG2 removes uracil bases from DNA which can appear through dUMP misincorporation or through cytosine deamination. If uracil is present instead of a cytosine, then the original GC pair becomes a GU pair. The uracil will then base pair to adenine in the replicated daughter strand. This results in a GC → AT mutation that could contribute to cancer formation.

RPA is known to target UNG2 towards individual uracil bases. We hypothesize that RPA will target UNG2 to uracil bases in DNA regardless of the number of uracils in the DNA strand.

 

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