Journal
PROTEIN SCIENCE
Volume 13, Issue 1, Pages 301-305Publisher
WILEY
DOI: 10.1110/ps.03319404
Keywords
O-6-alkylguanine-DNA alkyltransferase; O-6-methylguanine-methyltransferase; DNA binding; denaturation; protein-alkylation
Categories
Funding
- NATIONAL CANCER INSTITUTE [R37CA018137, R01CA018137] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [T32ES007312] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM008601] Funding Source: NIH RePORTER
- NCI NIH HHS [R37 CA018137, R01 CA018137, CA-18137] Funding Source: Medline
- NIEHS NIH HHS [T32 ES007312, 1 T32 ES-07312] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008601, GM-57906, R01 GM057906, 5 T32 GM-08601] Funding Source: Medline
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O-6-alkylguanine-DNA alkyltransferase (AGT) repairs pro-mutagenic O-6-alkylguanine and O-4-alkylthymine lesions in DNA. The alkylated form of the protein is not reactivated; instead, it is rapidly ubiquitinated and degraded. Here, we show that alkylation destabilizes the native fold of the protein by 0.5-1.2 kcal/mole and the DNA-binding function by 0.8-1.4 kcallmole. On this basis, we propose that destabilization of the native conformational ensemble acts as a signal for ubiquitination.
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