K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts

Autores
Wijeratne, Subhashinee S.K.; Camporeale, Gabriela; Zempleni, Janos
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Covalent modifications of histones play a role in regulating telomere attrition and cellular senescence. Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. We have previously shown that biotinylation of K12 in histone H4 (H4K12bio) is a marker for heterochromatin and is enriched in pericentromeric alpha satellite repeats. Here, we hypothesized that H4K12bio is also enriched in telomeres. We used human IMR-90 lung fibroblasts and immortalized IMR-90 cells overexpressing human telomerase (hTERT) in order to examine histone biotinylation in young and senescent cells. Our studies suggest that one out of three histone H4 molecules in telomeres is biotinylated at K12 in hTERT cells. The abundance of H4K12bio in telomeres decreased by 42% during telomere attrition in senescent IMR-90 cells; overexpression of telomerase prevented the loss of H4K12bio. Possible confounders such as decreased expression of HCS and biotin transporters were formally excluded in this study. Collectively, these data suggest that H4K12bio is enriched in telomeric repeats and represents a novel epigenetic mark for cell senescence.
Fil: Wijeratne, Subhashinee S.K.. University Of Nebraska; Estados Unidos
Fil: Camporeale, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. University Of Nebraska; Estados Unidos
Fil: Zempleni, Janos. University of Nebraska; Estados Unidos
Materia
Dna
Chromantin
Telomere
Histone
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/14577
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/14577
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblastsWijeratne, Subhashinee S.K.Camporeale, GabrielaZempleni, JanosDnaChromantinTelomereHistonehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Covalent modifications of histones play a role in regulating telomere attrition and cellular senescence. Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. We have previously shown that biotinylation of K12 in histone H4 (H4K12bio) is a marker for heterochromatin and is enriched in pericentromeric alpha satellite repeats. Here, we hypothesized that H4K12bio is also enriched in telomeres. We used human IMR-90 lung fibroblasts and immortalized IMR-90 cells overexpressing human telomerase (hTERT) in order to examine histone biotinylation in young and senescent cells. Our studies suggest that one out of three histone H4 molecules in telomeres is biotinylated at K12 in hTERT cells. The abundance of H4K12bio in telomeres decreased by 42% during telomere attrition in senescent IMR-90 cells; overexpression of telomerase prevented the loss of H4K12bio. Possible confounders such as decreased expression of HCS and biotin transporters were formally excluded in this study. Collectively, these data suggest that H4K12bio is enriched in telomeric repeats and represents a novel epigenetic mark for cell senescence.Fil: Wijeratne, Subhashinee S.K.. University Of Nebraska; Estados UnidosFil: Camporeale, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. University Of Nebraska; Estados UnidosFil: Zempleni, Janos. University of Nebraska; Estados UnidosElsevier2010-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14577Wijeratne, Subhashinee S.K.; Camporeale, Gabriela; Zempleni, Janos; K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts; Elsevier; Journal Of Nutritional Biochemistry; 21; 4; 4-2010; 310-3160955-2863enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0955286309000114info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jnutbio.2009.01.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:05:38Zoai:ri.conicet.gov.ar:11336/14577instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:05:38.737CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
title K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
spellingShingle K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
Wijeratne, Subhashinee S.K.
Dna
Chromantin
Telomere
Histone
title_short K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
title_full K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
title_fullStr K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
title_full_unstemmed K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
title_sort K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
dc.creator.none.fl_str_mv Wijeratne, Subhashinee S.K.
Camporeale, Gabriela
Zempleni, Janos
author Wijeratne, Subhashinee S.K.
author_facet Wijeratne, Subhashinee S.K.
Camporeale, Gabriela
Zempleni, Janos
author_role author
author2 Camporeale, Gabriela
Zempleni, Janos
author2_role author
author
dc.subject.none.fl_str_mv Dna
Chromantin
Telomere
Histone
topic Dna
Chromantin
Telomere
Histone
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Covalent modifications of histones play a role in regulating telomere attrition and cellular senescence. Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. We have previously shown that biotinylation of K12 in histone H4 (H4K12bio) is a marker for heterochromatin and is enriched in pericentromeric alpha satellite repeats. Here, we hypothesized that H4K12bio is also enriched in telomeres. We used human IMR-90 lung fibroblasts and immortalized IMR-90 cells overexpressing human telomerase (hTERT) in order to examine histone biotinylation in young and senescent cells. Our studies suggest that one out of three histone H4 molecules in telomeres is biotinylated at K12 in hTERT cells. The abundance of H4K12bio in telomeres decreased by 42% during telomere attrition in senescent IMR-90 cells; overexpression of telomerase prevented the loss of H4K12bio. Possible confounders such as decreased expression of HCS and biotin transporters were formally excluded in this study. Collectively, these data suggest that H4K12bio is enriched in telomeric repeats and represents a novel epigenetic mark for cell senescence.
Fil: Wijeratne, Subhashinee S.K.. University Of Nebraska; Estados Unidos
Fil: Camporeale, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. University Of Nebraska; Estados Unidos
Fil: Zempleni, Janos. University of Nebraska; Estados Unidos
description Covalent modifications of histones play a role in regulating telomere attrition and cellular senescence. Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. We have previously shown that biotinylation of K12 in histone H4 (H4K12bio) is a marker for heterochromatin and is enriched in pericentromeric alpha satellite repeats. Here, we hypothesized that H4K12bio is also enriched in telomeres. We used human IMR-90 lung fibroblasts and immortalized IMR-90 cells overexpressing human telomerase (hTERT) in order to examine histone biotinylation in young and senescent cells. Our studies suggest that one out of three histone H4 molecules in telomeres is biotinylated at K12 in hTERT cells. The abundance of H4K12bio in telomeres decreased by 42% during telomere attrition in senescent IMR-90 cells; overexpression of telomerase prevented the loss of H4K12bio. Possible confounders such as decreased expression of HCS and biotin transporters were formally excluded in this study. Collectively, these data suggest that H4K12bio is enriched in telomeric repeats and represents a novel epigenetic mark for cell senescence.
publishDate 2010
dc.date.none.fl_str_mv 2010-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/14577
Wijeratne, Subhashinee S.K.; Camporeale, Gabriela; Zempleni, Janos; K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts; Elsevier; Journal Of Nutritional Biochemistry; 21; 4; 4-2010; 310-316
0955-2863
url http://hdl.handle.net/11336/14577
identifier_str_mv Wijeratne, Subhashinee S.K.; Camporeale, Gabriela; Zempleni, Janos; K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts; Elsevier; Journal Of Nutritional Biochemistry; 21; 4; 4-2010; 310-316
0955-2863
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0955286309000114
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jnutbio.2009.01.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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