Herranz Martín, NicolásDave, NatàliaMillanes Romero, Alba, 1986-Morey Ramonell, LluísDíaz, Víctor M.Lórenz Fonfria, VíctorGutiérrez Gallego, Ricardo, 1968-Jerónimo, CeliaDi Croce, LucianoGarcía de Herreros, AntonioPeiró Sales, Sandra2015-12-112015-12-112012Herranz N, Dave N, Millanes-Romero A, Morey L, Díaz VM, Lórenz-Fonfría V et al. Lysyl oxidase-like 2 deaminates lysine 4 in histone H3. Molecular cell. 2012;46(3):369-76. DOI: 10.1016/j.molcel.2012.03.0021097-2765http://hdl.handle.net/10230/25392Methylation of lysine 4 (K4) within histone H3 has been linked to active transcription and is removed by LSD1 and the JmjC domain-containing proteins by amino-oxidation or hydroxylation, respectively. Here, we describe the deamination catalyzed by Lysyl oxidase-like 2 protein (LOXL2) as an unconventional chemical mechanism for H3K4 modification. Infrared spectroscopy and mass spectrometry analyses demonstrated that recombinant LOXL2 specifically deaminates trimethylated H3K4. Moreover, LOXL2 activity is linked with the transcriptional control of CDH1 gene by regulating H3K4me3 deamination. These results reveal another H3 modification and provide a different mechanism for H3K4 modification.application/pdfeng© Elsevier. This is the published version of an article http://dx.doi.org/10.1016/j.molcel.2012.03.002 that appeared in the journal Molecular cell. It is published in an Open Archive under an Elsevier user license. Details of this licence are available here: http://www.elsevier.com/about/open-access/open-access-policies/oa-license-policy/elsevier-user-licenseRegulació genèticaHistonesCadherinesinfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.molcel.2012.03.002info:eu-repo/semantics/openAccess