Lysyl oxidase-like 2 deaminates lysine 4 in histone H3

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dc.contributor.author	Herranz Martín, Nicolás
dc.contributor.author	Dave, Natàlia
dc.contributor.author	Millanes Romero, Alba, 1986-
dc.contributor.author	Morey Ramonell, Lluís
dc.contributor.author	Díaz, Víctor M.
dc.contributor.author	Lórenz Fonfria, Víctor
dc.contributor.author	Gutiérrez Gallego, Ricardo, 1968-
dc.contributor.author	Jerónimo, Celia
dc.contributor.author	Di Croce, Luciano
dc.contributor.author	García de Herreros, Antonio
dc.contributor.author	Peiró Sales, Sandra
dc.date	2012
dc.identifier.citation	Herranz 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): 369-376. DOI 10.1016/j.molcel.2012.03.002
dc.identifier.citation	1097-2765
dc.identifier.citation	http://dx.doi.org/10.1016/j.molcel.2012.03.002
dc.identifier.uri	http://hdl.handle.net/10230/25392
dc.format	application/pdf
dc.language.iso	eng
dc.publisher	American Society for Cell Biology
dc.relation	Molecular cell. 2012; 46(3): 369-376
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	© 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-license
dc.subject	Regulació genètica
dc.subject	Histones
dc.subject	Cadherines
dc.title	Lysyl oxidase-like 2 deaminates lysine 4 in histone H3
dc.type	info:eu-repo/semantics/article
dc.type	info:eu-repo/semantics/publishedVersion
dc.description.abstract	Methylation 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.

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