Date of Award
2002
Document Type
Honors Thesis (Open Access)
Department
Colby College. Chemistry Dept.
Advisor(s)
Julie T. Millard
Second Advisor
Shari U Dunham
Abstract
HMG1 is a nonhistone chromosomal protein that binds preferentially to some types of globally modified DNA. HMG1 has been implicated in the cellular response to the anti-cancer agent cisplatin, functioning to block excision repair of specific distorted platinated DNA lesions and resulting in enhanced cytotoxicity. We have investigated whether other DNA-binding agents also produce lesions that are recognized by HMG1. Specifically, we used polyacrylamide gel shift assays to monitor the potential HMG1 binding of diepoxybutane interstrand cross-links, which have been suggested to induce DNA bending. We isolated the native protein from chicken erythrocytes and expressed engineered HMG domain proteins in E. coli. Preliminary studies support weak. binding of the HMG A domain protein to the cross-linked DNA oligomer.
Keywords
Nucleoproteins -- Purification, Proteins -- Purification, Diepoxide DNA
Recommended Citation
Pageau, Gayle, "Purification of the HMG1 protein and investigation of its interactions with diepoxide cross-linked DNA" (2002). Honors Theses. Paper 193.https://digitalcommons.colby.edu/honorstheses/193
Copyright
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