User:Madelyn Kasprzak/Sandbox 1

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m (Added some additional notes to the end of the structure section and Fixed the double reference listing error)
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== Structure ==
== Structure ==
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The TET enzymes have a cysteine-rich region closely followed by a double stranded beta-helix (DSBH) domain near their C-terminus.<ref>DOI 10.1007/978-1-4419-9967-2_3</ref> The DSBH domain contains three Fe<sup>2+</sup> binding sites and an α-ketoglutarate binding site.<ref>DOI 10.1007/978-1-4419-9967-2_3</ref> This DSBH domain, along with the preceding cysteine-rich region, performs the main catalytic activity of these enzymes and more generally, for all α-ketoglutarate oxygenases. In addition, TET1 has a CXXC-type zinc finger domain near the N-terminus. However, the TET1 CXXC domain lacks the conserved lysine-phenylalanine-glycine-glycine (KFGG) motif commonly seen within the CXXC domains of other DNA binding proteins, such as DNA methyltransferase-1 (DNMT1). A study conducted by Frauer et al. in 2011 showed that the isolated CXXC domain of TET1 has no DNA binding activity, which agrees with the evidence suggesting that the KFGG motif increases affinity for unmethylated DNA.<ref>DOI 10.1371/journal.pone.0016627</ref>
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The TET enzymes have a cysteine-rich region closely followed by a double stranded beta-helix (DSBH) domain near their C-terminus.<ref name='Kinney et al.'>DOI 10.1007/978-1-4419-9967-2_3</ref> The DSBH domain contains three Fe<sup>2+</sup> binding sites and an α-ketoglutarate binding site.<ref name='Kinney et al.' /> This DSBH domain, along with the preceding cysteine-rich region, performs the main catalytic activity of these enzymes and more generally, for all α-ketoglutarate oxygenases. In addition, TET1 has a CXXC-type zinc finger domain near the N-terminus. However, the TET1 CXXC domain lacks the conserved lysine-phenylalanine-glycine-glycine (KFGG) motif commonly seen within the CXXC domains of other DNA binding proteins, such as DNA methyltransferase-1 (DNMT1). A study conducted by Frauer et al. in 2011 showed that the isolated CXXC domain of TET1 has no DNA binding activity, which agrees with the evidence suggesting that the KFGG motif increases affinity for unmethylated DNA.<ref name='Frauer et al.'>DOI 10.1371/journal.pone.0016627</ref> Frauer et al. also speculated that the CXXC domain of TET1 may be involved with protein-protein interactions instead of DNA binding.<ref name='Frauer et al.' />

Revision as of 00:58, 14 April 2016

TET Enzymes

TET-like protein in Naegleria gruberi in complex with DNA containing 5hmC.

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References

  1. ↑ Lorsbach RB, Moore J, Mathew S, Raimondi SC, Mukatira ST, Downing JR. TET1, a member of a novel protein family, is fused to MLL in acute myeloid leukemia containing the t(10;11)(q22;q23). Leukemia. 2003 Mar;17(3):637-41. PMID:12646957 doi:http://dx.doi.org/10.1038/sj.leu.2402834
  2. ↑ 2.0 2.1 Kinney SR, Pradhan S. Ten eleven translocation enzymes and 5-hydroxymethylation in mammalian development and cancer. Adv Exp Med Biol. 2013;754:57-79. doi: 10.1007/978-1-4419-9967-2_3. PMID:22956496 doi:http://dx.doi.org/10.1007/978-1-4419-9967-2_3
  3. ↑ 3.0 3.1 Frauer C, Rottach A, Meilinger D, Bultmann S, Fellinger K, Hasenoder S, Wang M, Qin W, Soding J, Spada F, Leonhardt H. Different binding properties and function of CXXC zinc finger domains in Dnmt1 and Tet1. PLoS One. 2011 Feb 2;6(2):e16627. doi: 10.1371/journal.pone.0016627. PMID:21311766 doi:http://dx.doi.org/10.1371/journal.pone.0016627

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Madelyn Kasprzak

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