Redox Potential Regulates Binding of Universal Minicircle Sequence Binding Protein at the Kinetoplast DNA Replication Origin

Volume 3, no. 2, p. 277–287, 2004. Page 284, Figure 10: In Fig. 10, we presented a result of an experiment with an N-terminally truncated universal minicircle sequence-binding protein (UMSBP) showing that binding of the mutated protein to UMS DNA was insensitive to oxidation. This observation could suggest that the N-terminal domain could serve in the redox-mediated regulation of UMSBP binding to DNA. However, we have recently found, reproducibly, that the UMSBP mutant lacking its N-terminal domain was redox sensitive, similar to the wild-type protein. This correction is limited to only this specific point in the article and does not alter the overall conclusions of our study.