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P.V. Tarlykov

RSE «National Center for Biotechnology» CSMESRK, Kurgalzhynskoye road, 13/5, Astana, 010000, Kazakhstan

A.B. Shevtsov

RSE «National Center for Biotechnology» CSMESRK, Kurgalzhynskoye road, 13/5, Astana, 010000, Kazakhstan

V.V. Ogryzko

Institut Gustave Roussy, CNRS UMR 8126, 114 Rue Edouard Vaillant, 94805, Villejuif, France

E.M. Ramanculov

RSE «National Center for Biotechnology» CSMESRK, Kurgalzhynskoye road, 13/5, Astana, 010000, Kazakhstan


One of the most promising areas of biology is the systematic approach to the study of chromatin, using new-generation sequencing and mass spectrometry. Our study proposes the use ofa previously developed technique, based on biotinylation of proteins that are inclose spatial proximitywith each other, for the study of DNA fragments co-precipitated during the pull-down of biotinylated proteins. We performed co-expression of the nuclear membrane protein emerin fused tobiotin ligase and hybrid histone mH2A fused to biotin acceptor (peptide specifically biotinylated by biotin ligase in the vicinity of the protein of interest). Using new-generation sequencing, we studied the chromatin in the vicinity of the nuclear envelope protein.This method has several advantages such as theability to utilize histone variants associated with specific functional states (e.g. active or repressed chromatin) and the possibility to perform pulse-chase experiments to monitor DNA sequences identified in proximity with lamin‑associated domains. Our work may throw light on the cellular mechanisms of chromatin remodelling and has important relevance for the understanding of different nuclear domains.


emerin, chromatin, biotin-ligase, biotinylation, western-blot, sequencing, lamin associated domain

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