Ravichandran, Mirunalini ; Rafalski, Dominik ; Davies, Claudia I. ; Ortega-Recalde, Oscar 
; Nan, Xinsheng ; Glanfield, Cassandra R. ; Kotter, Annika ; Misztal, Katarzyna ; Wang, Andrew H. ; Wojciechowski, Marek ; Rażew, Michał ; Mayyas, Issam M. ; Kardailsky, Olga ; Schwartz, Uwe ; Zembrzycki, Krzysztof ; Morison, Ian M. ; Helm, Mark ; Weichenhan, Dieter ; Jurkowska, Renata Z. ; Krueger, Felix ; Plass, Christoph ; Zacharias, Martin ; Bochtler, Matthias ; Hore, Timothy A. ; Jurkowski, Tomasz P.
; Nan, Xinsheng ; Glanfield, Cassandra R. ; Kotter, Annika ; Misztal, Katarzyna ; Wang, Andrew H. ; Wojciechowski, Marek ; Rażew, Michał ; Mayyas, Issam M. ; Kardailsky, Olga ; Schwartz, Uwe ; Zembrzycki, Krzysztof ; Morison, Ian M. ; Helm, Mark ; Weichenhan, Dieter ; Jurkowska, Renata Z. ; Krueger, Felix ; Plass, Christoph ; Zacharias, Martin ; Bochtler, Matthias ; Hore, Timothy A. ; Jurkowski, Tomasz P. 
Zusammenfassung
TET (ten-eleven translocation) enzymes catalyze the oxidation of 5-methylcytosine bases in DNA, thus driving active and passive DNA demethylation. Here, we report that the catalytic domain of mammalian TET enzymes favor CGs embedded within basic helix-loop-helix and basic leucine zipper domain transcription factor-binding sites, with up to 250-fold preference in vitro. Crystal structures and ...
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