Binding of the J-Binding Protein to DNA Containing Glucosylated hmU (Base J) or 5-hmC: Evidence for a Rapid Conformational Change upon DNA Binding
Author:
Affiliation:
1. Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712, United States
2. Institut Laue-Langevin, 6 rue Jules Horowitz, BP 156, 38042 Grenoble Cedex 9, France
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja303423t
Reference41 articles.
1. The modified base J is the target for a novelDNA-binding protein in kinetoplastid protozoans
2. Regulation of Trypanosome DNA Glycosylation by a SWI2/SNF2-like Protein
3. JBP2, a SWI2/SNF2-like protein, regulates de novo telomeric DNA glycosylation in bloodstream form Trypanosoma brucei
4. Evidence that J-binding protein 2 is a thymidine hydroxylase catalyzing the first step in the biosynthesis of DNA base J
5. The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase
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1. Distant sequence regions of JBP1 contribute to J-DNA binding;Life Science Alliance;2023-06-16
2. Behind Base J: The Roles of JBP1 and JBP2 on Trypanosomatids;Pathogens;2023-03-16
3. Distant sequence regions of JBP1 contribute to J-DNA binding;2023-01-24
4. The domain architecture of the protozoan protein J-DNA–binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity;Journal of Biological Chemistry;2019-08
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