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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
14/02/2013 |
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Data da última atualização: |
08/01/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
BITAR, M.; DRUMMOND, M. G.; COSTA, M. G. S.; LOBO, F. P.; CALZAVARA-SILVA, C. E.; BISCH, P. M.; MACHADO, C. R.; MACEDO, A. M.; PIERCE, R. J.; FRANCO, G. R. |
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Afiliação: |
MAINÁ BITAR, UFRJ, UFMG; MARCELA GONÇALVES DRUMMOND, UFMG, Univ. Lille Nord de France; MAURICIO GARCIA SOUZA COSTA, UFRJ; FRANCISCO PEREIRA LOBO, CNPTIA; CARLOS EDUARDO CALZAVARA-SILVA, Fiocruz; PAULO MASCARELLO BISCH, UFRJ; CARLOS RENATO MACHADO, UFMG; ANDRÉA MARA MACEDO, UFMG; RAYMOND J. PIERCE, Univ. Lille Nord de France; GLÓRIA REGINA FRANCO, UFMG. |
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Título: |
Modeling the zing finger protein SmZF1 from Schistosoma mansoni: Insights into DNA binding and gene regulation. |
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Ano de publicação: |
2013 |
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Fonte/Imprenta: |
Journal of Molecular Graphics and Modelling, New York, v. 39, p. 29-38, 2013. |
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Idioma: |
Inglês |
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Conteúdo: |
Zinc finger proteins are widely found in eukaryotes, representing an important class of DNA-binding proteins frequently involved in transcriptional regulation. Zinc finger motifs are composed by two antiparallel b-strands and one a-helix, stabilized by a zinc ion coordinated by conserved histidine and cysteine residues. In Schistosoma mansoni, these regulatory proteins are known to modulate morphological and physiological changes, having crucial roles in parasite development. A previously described C2H2 zinc finger protein, SmZF1, was shown to be present in cell nuclei of different life stages of S. mansoni and to activate gene transcription in a heterologous system. A high-quality SmZF1 tridimensional structure was generated using comparative modeling. Molecular dynamics simulations of the obtained structure revealed stability of the zinc fingers motifs and high flexibility on the terminals, comparable to the profile observed on the template X-ray structure based on thermal b-factors. Based on the protein tridimensional features and amino acid composition, we were able to characterize four C2 H2 zinc finger motifs, the first involved in protein?protein interactions while the three others involved in DNA binding. We defined a consensus DNA binding sequence using three distinct algorithms and further carried out docking calculations, which revealed the interaction of fingers 2?4 with the predicted DNA. A search for S. mansoni genes presenting putative SmZF1 binding sites revealed 415 genes hypothetically under SmZF1 control. Using an automatic annotation and GO assignment approach, we found that the majority of those genes code for proteins involved in developmental processes. Taken together, these results present a consistent base to the structural and functional characterization of SmZF1. MenosZinc finger proteins are widely found in eukaryotes, representing an important class of DNA-binding proteins frequently involved in transcriptional regulation. Zinc finger motifs are composed by two antiparallel b-strands and one a-helix, stabilized by a zinc ion coordinated by conserved histidine and cysteine residues. In Schistosoma mansoni, these regulatory proteins are known to modulate morphological and physiological changes, having crucial roles in parasite development. A previously described C2H2 zinc finger protein, SmZF1, was shown to be present in cell nuclei of different life stages of S. mansoni and to activate gene transcription in a heterologous system. A high-quality SmZF1 tridimensional structure was generated using comparative modeling. Molecular dynamics simulations of the obtained structure revealed stability of the zinc fingers motifs and high flexibility on the terminals, comparable to the profile observed on the template X-ray structure based on thermal b-factors. Based on the protein tridimensional features and amino acid composition, we were able to characterize four C2 H2 zinc finger motifs, the first involved in protein?protein interactions while the three others involved in DNA binding. We defined a consensus DNA binding sequence using three distinct algorithms and further carried out docking calculations, which revealed the interaction of fingers 2?4 with the predicted DNA. A search for S. mansoni genes presenting putative SmZF1 binding sites reve... Mostrar Tudo |
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Palavras-Chave: |
Ligação de DNA; Regulação gênica. |
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Thesagro: |
Schistosoma Mansoni. |
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Thesaurus Nal: |
DNA-binding proteins; Gene expression regulation; Zinc finger motif. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02751naa a2200301 a 4500
001 1949183
005 2020-01-08
008 2013 bl uuuu u00u1 u #d
100 1 $aBITAR, M.
245 $aModeling the zing finger protein SmZF1 from Schistosoma mansoni$bInsights into DNA binding and gene regulation.$h[electronic resource]
260 $c2013
520 $aZinc finger proteins are widely found in eukaryotes, representing an important class of DNA-binding proteins frequently involved in transcriptional regulation. Zinc finger motifs are composed by two antiparallel b-strands and one a-helix, stabilized by a zinc ion coordinated by conserved histidine and cysteine residues. In Schistosoma mansoni, these regulatory proteins are known to modulate morphological and physiological changes, having crucial roles in parasite development. A previously described C2H2 zinc finger protein, SmZF1, was shown to be present in cell nuclei of different life stages of S. mansoni and to activate gene transcription in a heterologous system. A high-quality SmZF1 tridimensional structure was generated using comparative modeling. Molecular dynamics simulations of the obtained structure revealed stability of the zinc fingers motifs and high flexibility on the terminals, comparable to the profile observed on the template X-ray structure based on thermal b-factors. Based on the protein tridimensional features and amino acid composition, we were able to characterize four C2 H2 zinc finger motifs, the first involved in protein?protein interactions while the three others involved in DNA binding. We defined a consensus DNA binding sequence using three distinct algorithms and further carried out docking calculations, which revealed the interaction of fingers 2?4 with the predicted DNA. A search for S. mansoni genes presenting putative SmZF1 binding sites revealed 415 genes hypothetically under SmZF1 control. Using an automatic annotation and GO assignment approach, we found that the majority of those genes code for proteins involved in developmental processes. Taken together, these results present a consistent base to the structural and functional characterization of SmZF1.
650 $aDNA-binding proteins
650 $aGene expression regulation
650 $aZinc finger motif
650 $aSchistosoma Mansoni
653 $aLigação de DNA
653 $aRegulação gênica
700 1 $aDRUMMOND, M. G.
700 1 $aCOSTA, M. G. S.
700 1 $aLOBO, F. P.
700 1 $aCALZAVARA-SILVA, C. E.
700 1 $aBISCH, P. M.
700 1 $aMACHADO, C. R.
700 1 $aMACEDO, A. M.
700 1 $aPIERCE, R. J.
700 1 $aFRANCO, G. R.
773 $tJournal of Molecular Graphics and Modelling, New York$gv. 39, p. 29-38, 2013.
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Embrapa Agricultura Digital (CNPTIA) |
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Registro Completo
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Biblioteca(s): |
Embrapa Agroindústria Tropical. |
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Data corrente: |
23/02/2022 |
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Data da última atualização: |
23/02/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
NASCIMENTO, R. J. M.; BEZERRA, L. C. A.; ALMEIDA, J. S.; BARROS, M. DE O.; SILVA, L. R. R.; ROSA, M. de F.; MAZZETO, S. E.; LOMONACO, D.; PEREIRA, K. R. A.; AVELINO, F. |
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Afiliação: |
ROGÉRIO JOSÉ MELO NASCIMENTO, Federal Institute of Education, Science and Technology of Ceará, Iguatu; LUIZ CARLOS ALVES BEZERRA, Federal Institute of Education, Science and Technology of Ceará, Iguatu; JÉSSICA SILVA ALMEIDA, Departament of Chemical Engineering, Federal University of Ceará; MATHEUS DE OLIVEIRA BARROS, Departament of Organic and Inorganic Chemistry, Federal University of Ceará; LUCAS RENAN ROCHA SILVA, Departament of Organic and Inorganic Chemistry, Federal University of Ceará; MORSYLEIDE DE FREITAS ROSA, CNPAT; SELMA ELAINE MAZZETO, Departament of Organic and Inorganic Chemistry, Federal University of Ceará; DIEGO LOMONACO, Departament of Organic and Inorganic Chemistry, Federal University of Ceará; KILTON RENAN ALVES PEREIRA, Federal Institute of Education, Science and Technology of Ceará, Iguatu; FRANCISCO AVELINO, Federal Institute of Education, Science and Technology of Ceará, Iguatu. |
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Título: |
Elucidating the adsorption mechanism of Rhodamine B on mesoporous coconut coir?based biosorbents through a non?linear modeling and recycling approach. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Environmental Science and Pollution Research, jan. 2022. |
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DOI: |
https://doi.org/10.1007/s11356-022-18808-9 |
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Idioma: |
Inglês |
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Palavras-Chave: |
Agro-resíduos; Agro-waste; Biorefinery; Biorrefinaria; Corantes têxteis; Environmental pollution; Textile dye. |
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Thesagro: |
Poluição Ambiental. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01045naa a2200325 a 4500
001 2140333
005 2022-02-23
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1007/s11356-022-18808-9$2DOI
100 1 $aNASCIMENTO, R. J. M.
245 $aElucidating the adsorption mechanism of Rhodamine B on mesoporous coconut coir?based biosorbents through a non?linear modeling and recycling approach.$h[electronic resource]
260 $c2022
650 $aPoluição Ambiental
653 $aAgro-resíduos
653 $aAgro-waste
653 $aBiorefinery
653 $aBiorrefinaria
653 $aCorantes têxteis
653 $aEnvironmental pollution
653 $aTextile dye
700 1 $aBEZERRA, L. C. A.
700 1 $aALMEIDA, J. S.
700 1 $aBARROS, M. DE O.
700 1 $aSILVA, L. R. R.
700 1 $aROSA, M. de F.
700 1 $aMAZZETO, S. E.
700 1 $aLOMONACO, D.
700 1 $aPEREIRA, K. R. A.
700 1 $aAVELINO, F.
773 $tEnvironmental Science and Pollution Research, jan. 2022.
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Embrapa Agroindústria Tropical (CNPAT) |
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