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Functional studies of human polymerase η A264P (736.6)
Author(s) -
Lentscher Anthony,
Jiang Xiaohua
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.736.6
Subject(s) - xeroderma pigmentosum , dna polymerase , mutagenesis , polymerase , dna replication , pyrimidine dimer , dna repair , dna polymerase ii , dna polymerase i , dna , dna clamp , mutation , nucleotide excision repair , dna damage , mutant , biology , transformation (genetics) , microbiology and biotechnology , genetics , polymerase chain reaction , gene , reverse transcriptase
DNA is the blueprint which contains the information necessary for a cell to maintain normal structure and function. This essential function of DNA means the cell must necessarily preserve the integrity of its blueprint. Harmful mutations must be minimalized where they cannot be completely eliminated. One such method for maintaining the integrity of DNA is through the function of human polymerase η, a replication enzyme which gains its utility in its ability to correct thymine dimerization mutations to DNA as a result of exposure to ultraviolet radiation. Mutations in human polymerase η lead to a xeroderma pigmentosum variant (XPV) which is limited in its ability to repair damage done to DNA. This research will include introducing the A264P mutation to the catalytic core of the enzyme through site‐directed mutagenesis, transformation of the resultant DNA into E. coli cells, eventually to overexpress and purify the protein, and run translesion synthesis assays in order to determine how restricted the function of the A264P mutant is when compared to the wild‐type protein.