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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: |
LEADER 02780naa a2200301 a 4500
001 1986615
005 2024-02-05
008 2014 bl uuuu u00u1 u #d
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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Embrapa Gado de Leite (CNPGL) |
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Registro Completo
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
10/10/2008 |
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Data da última atualização: |
20/09/2017 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
VIANA, P. A. |
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Afiliação: |
PAULO AFONSO VIANA, CNPMS. |
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Título: |
Atualidades de RPI no Brasil: melhoramento clássico e OGM - milho. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 22., 2008, Uberlândia. Ciência, tecnologia e inovação: resumos... Viçosa: UFV, 2008. |
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Descrição Física: |
1 CD-ROM. |
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Idioma: |
Português |
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Notas: |
Resumo ID: 2460-2 |
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Thesagro: |
Milho; Zea mays. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/35919/1/Atualidades-RPI.pdf
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Marc: |
LEADER 00511nam a2200145 a 4500
001 1491371
005 2017-09-20
008 2008 bl uuuu u00u1 u #d
100 1 $aVIANA, P. A.
245 $aAtualidades de RPI no Brasil$bmelhoramento clássico e OGM - milho.$h[electronic resource]
260 $aIn: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 22., 2008, Uberlândia. Ciência, tecnologia e inovação: resumos... Viçosa: UFV$c2008
300 $c1 CD-ROM.
500 $aResumo ID: 2460-2
650 $aMilho
650 $aZea mays
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