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000491473 0247_ $$2doi$$a10.1126/sciadv.abm2427
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000491473 1001_ $$00000-0002-1991-5695$$aRavichandran, Mirunalini$$b0
000491473 245__ $$aPronounced sequence specificity of the TET enzyme catalytic domain guides its cellular function
000491473 260__ $$aWashington, DC [u.a.]$$bAssoc.$$c2022
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000491473 520__ $$aTET (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 molecular dynamics calculations show that sequence preference is caused by intrasubstrate interactions and CG flanking sequence indirectly affecting enzyme conformation. TET sequence preferences are physiologically relevant as they explain the rates of DNA demethylation in TET-rescue experiments in culture and in vivo within the zygote and germ line. Most and least favorable TET motifs represent DNA sites that are bound by methylation-sensitive immediate-early transcription factors and octamer-binding transcription factor 4 (OCT4), respectively, illuminating TET function in transcriptional responses and pluripotency support. 
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000491473 7001_ $$00000-0002-3449-7460$$aRafalski, Dominik$$b1
000491473 7001_ $$00000-0001-7416-3249$$aDavies, Claudia I.$$b2
000491473 7001_ $$00000-0002-8076-0346$$aOrtega-Recalde, Oscar$$b3
000491473 7001_ $$00000-0002-0865-7934$$aNan, Xinsheng$$b4
000491473 7001_ $$00000-0002-2049-8585$$aGlanfield, Cassandra R.$$b5
000491473 7001_ $$0P:(DE-HGF)0$$aKotter, Annika$$b6
000491473 7001_ $$00000-0001-6575-2500$$aMisztal, Katarzyna$$b7
000491473 7001_ $$0P:(DE-HGF)0$$aWang, Andrew H.$$b8
000491473 7001_ $$0P:(DE-H253)PIP1011597$$aWojciechowski, Marek$$b9
000491473 7001_ $$00000-0003-1306-4743$$aRażew, Michał$$b10
000491473 7001_ $$0P:(DE-HGF)0$$aMayyas, Issam M.$$b11
000491473 7001_ $$0P:(DE-HGF)0$$aKardailsky, Olga$$b12
000491473 7001_ $$00000-0002-7628-2687$$aSchwartz, Uwe$$b13
000491473 7001_ $$00000-0001-7693-174X$$aZembrzycki, Krzysztof$$b14
000491473 7001_ $$00000-0003-3616-0025$$aMorison, Ian M.$$b15
000491473 7001_ $$00000-0002-0154-0928$$aHelm, Mark$$b16
000491473 7001_ $$0P:(DE-HGF)0$$aWeichenhan, Dieter$$b17
000491473 7001_ $$00000-0002-4507-2222$$aJurkowska, Renata Z.$$b18
000491473 7001_ $$00000-0002-5513-3324$$aKrueger, Felix$$b19
000491473 7001_ $$00000-0003-2554-3952$$aPlass, Christoph$$b20
000491473 7001_ $$00000-0001-5163-2663$$aZacharias, Martin$$b21
000491473 7001_ $$0P:(DE-H253)PIP1011590$$aBochtler, Matthias$$b22
000491473 7001_ $$00000-0002-6735-225X$$aHore, Timothy A.$$b23$$eCorresponding author
000491473 7001_ $$00000-0002-2012-0240$$aJurkowski, Tomasz P.$$b24$$eCorresponding author
000491473 773__ $$0PERI:(DE-600)2810933-8$$a10.1126/sciadv.abm2427$$gVol. 8, no. 36, p. eabm2427$$n36$$peabm2427$$tScience advances$$v8$$x2375-2548$$y2022
000491473 8564_ $$uhttps://www.science.org/doi/10.1126/sciadv.abm2427?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%20%200pubmed
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