Quantitative and kinetic single-molecule analysis of DNA unwinding by <i>Escherichia coli</i> UvrD helicase
Author:
Affiliation:
1. The Graduate School for the Creation of New Photonics Industries
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/19/0/19_e190006/_pdf
Reference51 articles.
1. [1] Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D. DNA Repair and Mutagenesis: Second edition (ASM Press, Washington D.C., 2005).
2. [2] Yokota, H. DNA unwinding and oligomerization dynamics of Escherichia coli UvrD helicase revealed by single-molecule fluorescence imaging. SEIBUTSU BUTSURI 61, 227–231 (2021). https://doi.org/10.2142/biophys.61.227
3. [3] Singleton, M. R., Dillingham, M. S., Wigley, D. B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76, 23–50 (2007). https://doi.org/10.1146/annurev.biochem.76.052305.115300
4. [4] Singleton, M. R., Sawaya, M. R., Ellenberger, T., Wigley, D. B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589–600 (2000). https://doi.org/10.1016/S0092-8674(00)80871-5
5. [5] Enemark, E. J., Joshua-Tor, L. On helicases and other motor proteins. Curr. Opin. Struct. Biol. 18, 243–257 (2008). https://doi.org/10.1016/j.sbi.2008.01.007
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