Site-Directed Mutagenesis of the REV1 BRCT Domain
Conference Year
2024
Abstract
The translesion synthesis (TLS) polymerase REV1 modulates error-prone replication of DNA and contains a BRCT domain that interacts with proliferating cell nuclear antigen (PCNA). Structural analysis has identified five amino acid residues within the BRCT domain that are critical to the BRCT-PCNA interaction. Site-directed mutagenesis was used to generate point mutants for the five amino acid residues and Sanger sequencing confirmed successful generation of the R68A, G76R, Y81A, and K86A point mutants. These point mutants provide a useful tool for investigating the in vitro significance of the BRCT-PCNA interaction on TLS.
Primary Faculty Mentor Name
Nimrat Chatterjee
Status
Undergraduate
Student College
College of Arts and Sciences
Program/Major
Biochemistry
Primary Research Category
Life Sciences
Site-Directed Mutagenesis of the REV1 BRCT Domain
The translesion synthesis (TLS) polymerase REV1 modulates error-prone replication of DNA and contains a BRCT domain that interacts with proliferating cell nuclear antigen (PCNA). Structural analysis has identified five amino acid residues within the BRCT domain that are critical to the BRCT-PCNA interaction. Site-directed mutagenesis was used to generate point mutants for the five amino acid residues and Sanger sequencing confirmed successful generation of the R68A, G76R, Y81A, and K86A point mutants. These point mutants provide a useful tool for investigating the in vitro significance of the BRCT-PCNA interaction on TLS.