Journal
ACS CHEMICAL BIOLOGY
Volume 9, Issue 8, Pages 1685-1691Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb500133k
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Funding
- U.S. National Science Foundation [MCB-0953764]
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Polyubiquitination of proteins regulates a variety of cellular processes, including protein degradation, NF-kappa B pathway activation, apoptosis, and DNA damage tolerance. Methods for generating polyubiquitinated protein with defined ubiquitin chain linkage and length are needed for an in-depth molecular understanding of protein polyubiquitination. However, enzymatic protein polyubiquitination usually generates polyubiquitinated proteins with mixed chain lengths in a low yield. We report herein a new chemical approach for protein polyubiquitination with a defined ubiquitin chain length and linkage under a mild condition that preserves the native fold of the target protein. In DNA damage tolerance, K63-polyubiquitinated proliferating cell nuclear antigen (PCNA) plays an important yet unclear role in regulating the selection of the error-free over error-prone lesion bypass pathways. Using the chemically polyubiquitinated PCNA, we revealed a mechanism of the K63 polyubiquitin chain on PCNA in promoting the error-free lesion bypass by suppressing the DNA translesion synthesis (TLS).
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