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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
20/05/2014 |
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Data da última atualização: |
05/02/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
CHRISTOPHOROU, M. A.; CASTELO-BRANCO, G.; HALLEY-STOTT, R. P.; OLIVEIRA, C. S.; LOOS, R.; RADZISHEUSKAYA, A.; MOWEN, K. A.; BERTONE, P.; SILVA, J. C. R.; ZERNICKA-GOETZ, M.; MICHAEL L. NIELSEN; GURDON, J. B.; KOUZARIDES, T. |
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Afiliação: |
MARIA A. CHRISTOPHOROU, University of Cambridge; GONÇALO CASTELO-BRANCO, University of Cambridge; Karolinska Institutet, Stockholm, Sweden; RICHARD P. HALLEY-STOTT, University of Cambridge; CLARA SLADE OLIVEIRA, CNPGL; REMCO LOOS, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge; ALIAKSANDRA RADZISHEUSKAYA, University of Cambridge; KERRI A. MOWEN, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California; PAUL BERTONE, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge; University of Cambridge; JOSÉ C. R. SILVA, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge , University of Cambridge.; MAGDALENA ZERNICKA-GOETZ, University of Cambridge; NIELSEN, M. L., University of Copenhagen,Copenhagen, Denmark; JOHN B. GURDON, University of Cambridge; TONY KOUZARIDES, University of Cambridge. |
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Título: |
Citrullination regulates pluripotency and histone H1 binding to chromatin |
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Ano de publicação: |
2014 |
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Fonte/Imprenta: |
Nature, v. 507, n. 7490, p. 104-108, 2014. |
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DOI: |
https://doi.org/10.1038/nature12942 |
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Idioma: |
Inglês |
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Conteúdo: |
Citrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of compact chromatin, as novel PADI4 substrates. Citrullination of a single arginine residue within the DNA-binding site of H1 results in its displacement from chromatin and global chromatin decondensation. Together, these results uncover a role for citrullination in the regulation of pluripotency and provide new mechanistic insights into how citrullination regulates chromatin compaction. MenosCitrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of com... Mostrar Tudo |
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Palavras-Chave: |
Histone post-translational modifications; Reprogramming. |
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Categoria do assunto: |
W Química e Física |
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Marc: |
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001 1986615
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024 7 $ahttps://doi.org/10.1038/nature12942$2DOI
100 1 $aCHRISTOPHOROU, M. A.
245 $aCitrullination regulates pluripotency and histone H1 binding to chromatin$h[electronic resource]
260 $c2014
520 $aCitrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of compact chromatin, as novel PADI4 substrates. Citrullination of a single arginine residue within the DNA-binding site of H1 results in its displacement from chromatin and global chromatin decondensation. Together, these results uncover a role for citrullination in the regulation of pluripotency and provide new mechanistic insights into how citrullination regulates chromatin compaction.
653 $aHistone post-translational modifications
653 $aReprogramming
700 1 $aCASTELO-BRANCO, G.
700 1 $aHALLEY-STOTT, R. P.
700 1 $aOLIVEIRA, C. S.
700 1 $aLOOS, R.
700 1 $aRADZISHEUSKAYA, A.
700 1 $aMOWEN, K. A.
700 1 $aBERTONE, P.
700 1 $aSILVA, J. C. R.
700 1 $aZERNICKA-GOETZ, M.
700 1 $aMICHAEL L. NIELSEN
700 1 $aGURDON, J. B.
700 1 $aKOUZARIDES, T.
773 $tNature$gv. 507, n. 7490, p. 104-108, 2014.
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| 5. |  | ANDRADE, L. H. M.; LUGARINI, C.; OLIVEIRA, R. A. S.; SILVA, L. T. R.; MARVULO, M. F. V.; GARCIA, J. E.; DUBEY, J. P.; SILVA, J. C. R. Ocorrência de anticorpos anti-Toxoplasma gondii em aves silvestres de três Unidades de Conservação Federais da Paraíba e da Bahia. Pesquisa Veterinária Brasileira,Rio de Janeiro, v. 36, n. 2, p. 103-107, fev. 2016.| Biblioteca(s): Embrapa Unidades Centrais. |
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| 6. | | FERRONATO, J.; SANTOS, L. P. dos; FERREIRA, K. G. G.; SILVA, J. C. R. L.; MAZZOCATO, A. C.; ROCHA, D. S. da; KÖPP, M. M.; FERREIRA, J. L. Mapeamento de coletas antigas de acessos de espécies forrageiras nativas do Sul do Brasil. In: CONGRESSO BRASILEIRO DE ZOOTECNIA, 26., 2016, Santa Maria. Cinquenta anos de zootecnia no Brasil: anais. Santa Maria: Sociedade Brasileira de Zootecnia, 2016. Zootec.| Tipo: Artigo em Anais de Congresso |
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| 7. | | PRATES, F. B. de S.; PALERMO, D. P.; SILVA, J. C. R. da; DONAGEMMA, G. K.; CRUZ, G. G. da; ZONTA, E. Teores de Fósforo em Plantas de Pinhão Manso submetido a doses de Alumínio em cultivo Hidropônico. In: CONGRESSO BRASILEIRO DE CIÊNCIAS DO SOLO, 34., 2013. Florianópolis. Anais... Viçosa, MG: Sociedade Brasileira de Cência do Solo, 2013. 4 p.| Tipo: Artigo em Anais de Congresso |
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| 8. | | CHRISTOPHOROU, M. A.; CASTELO-BRANCO, G.; HALLEY-STOTT, R. P.; OLIVEIRA, C. S.; LOOS, R.; RADZISHEUSKAYA, A.; MOWEN, K. A.; BERTONE, P.; SILVA, J. C. R.; ZERNICKA-GOETZ, M.; MICHAEL L. NIELSEN; GURDON, J. B.; KOUZARIDES, T. Citrullination regulates pluripotency and histone H1 binding to chromatin Nature, v. 507, n. 7490, p. 104-108, 2014.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
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| 9. | | RITTER, R. A.; MONTEIRO, M. V. B.; MONTEIRO, F. O. B.; RODRIGUES, S. T.; SOARES, M. L.; SILVA J. C. R.; PALHA, M. das D. C.; BIONDI, G. F.; RAHAL, S. C.; TOURINHO, M. M. Ethnoveterinary knowledge and practices at Colares island, Pará state, eastern Amazon, Brazil. Journal of Ethnopharmacology, v. 144, n. 2, p. 346-352, Nov. 2012.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 10. | | FERREIRA, J. L.; GWINNER, R.; FERREIRA, L. M.; FERRONATO, J.; LEITE, L. G.; FERREIRA, K. G. G.; SILVA, J. C. R. L.; SANTOS, L. P. dos; SILVA, A. W. T. Understanding the extent of phenotypic variability in accessions of Paspalum urvillei Steud. from the USDA NPGS. Iheringia: série botânica, v. 75, e2020006, 2020.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 1 |
| Biblioteca(s): Embrapa Pecuária Sul. |
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| 11. | | HOMEM, V. S. F.; HEINEMANN, M. B.; MORAES, Z. M.; VIANNA, M. C. B.; SILVA, J. C. R.; SAKAMOTO, S. M.; PINHEIRO, S. R.; VEIGA, J. B. da; LAU, H. D.; QUANZ, D.; TOURRAND, J.-F.; FERREIRA, F.; FERREIRA NETO, J. S. Leptospirose bovina em Uruará, PA, município da Amazônia Oriental. Arquivos do Instituto Biológico, v. 67, n. 1, p. 1-10, 2000.| Biblioteca(s): Embrapa Amazônia Oriental. |
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