Base de dados : LILACS
Pesquisa : G02.111.570.820.709.275.750.500 [Categoria DeCS]
Referências encontradas : 4 [refinar]
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Id: biblio-1040227
Autor: Shu, Xuan; Dong, Zejun; Cheng, Liuhanghang; Shu, Shenyou.
Título: DNA hypermethylation of Fgf16 and Tbx22 associated with cleft palate during palatal fusion
Fonte: J. appl. oral sci;27:e20180649, 2019. graf.
Idioma: en.
Projeto: National Science Foundation of China; . Natural Science Foundation of Guangdong Province.
Resumo: Abstract Objective: Cleft palate (CP) is a congenital birth defect caused by the failure of palatal fusion. Little is known about the potential role of DNA methylation in the pathogenesis of CP. This study aimed to explore the potential role of DNA methylation in the mechanism of CP. Methodology: We established an all-trans retinoic acid (ATRA)-induced CP model in C57BL/6J mice and used methylation-dependent restriction enzymes (MethylRAD, FspEI) combined with high-throughput sequencing (HiSeq X Ten) to compare genome-wide DNA methylation profiles of embryonic mouse palatal tissues, between embryos from ATRA-treated vs. untreated mice, at embryonic gestation day 14.5 (E14.5) (n=3 per group). To confirm differentially methylated levels of susceptible genes, real-time quantitative PCR (qPCR) was used to correlate expression of differentially methylated genes related to CP. Results: We identified 196 differentially methylated genes, including 17,298 differentially methylated CCGG sites between ATRA-treated vs. untreated embryonic mouse palatal tissues (P<0.05, log2FC>1). The CP-related genes Fgf16 (P=0.008, log2FC=1.13) and Tbx22 (P=0.011, log2FC=1.64,) were hypermethylated. Analysis of Fgf16 and Tbx22, using Gene Ontology (GO) and the Kyoto Encyclopedia of Genes and Genomes (KEGG), identified 3 GO terms and 1 KEGG pathway functionally related to palatal fusion. The qPCR showed that changes in expression level negatively correlated with methylation levels. Conclusions: Taken together, these results suggest that hypermethylation of Fgf16 and Tbx22 is associated with decreased gene expression, which might be responsible for developmental failure of palatal fusion, eventually resulting in the formation of CP.
Descritores: Fissura Palatina/genética
Metilação de DNA
Proteínas com Domínio T/genética
Fatores de Crescimento de Fibroblastos/genética
-Valores de Referência
Expressão Gênica
Fissura Palatina/embriologia
Fissura Palatina/patologia
Análise de Sequência de DNA
Proteínas com Domínio T/análise
Domínios e Motivos de Interação entre Proteínas
Reação em Cadeia da Polimerase em Tempo Real
Fatores de Crescimento de Fibroblastos/análise
Camundongos Endogâmicos C57BL
Limites: Animais
Masculino
Feminino
Responsável: BR28.1 - Serviço de Biblioteca e Documentação Professor Doutor Antônio Gabriel Atta


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Buzalaf, Marilia Afonso Rabelo
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Id: lil-787547
Autor: KHAN, Zohaib Nisar; LEITE, Aline de Lima; CHARONE, Senda; SABINO, Isabela Tomazini; MARTINI, Tatiana; PEREIRA, Heloísa Aparecida Barbosa da Silva; OLIVEIRA, Rodrigo Cardoso; BUZALAF, Marília Afonso Rabelo.
Título: Liver proteome of mice with different genetic susceptibilities to the effects of fluoride
Fonte: J. appl. oral sci;24(3):250-257tab, graf.
Idioma: en.
Resumo: ABSTRACT A/J and 129P3/J mice strains have been widely studied over the last few years because they respond quite differently to fluoride (F) exposure. 129P3/J mice are remarkably resistant to the development of dental fluorosis, despite excreting less F in urine and having higher circulating F levels. These two strains also present different characteristics regardless of F exposure. Objective In this study, we investigated the differential pattern of protein expression in the liver of these mice to provide insights on why they have different responses to F. Material and Methods Weanling male A/J and 129P3/J mice (n=10 from each strain) were pared and housed in metabolic cages with ad libitum access to low-F food and deionized water for 42 days. Liver proteome profiles were examined using nLC-MS/MS. Protein function was classified by GO biological process (Cluego v2.0.7 + Clupedia v1.0.8) and protein-protein interaction network was constructed (PSICQUIC, Cytoscape). Results Most proteins with fold change were increased in A/J mice. The functional category with the highest percentage of altered genes was oxidation-reduction process (20%). Subnetwork analysis revealed that proteins with fold change interacted with Disks large homolog 4 and Calcium-activated potassium channel subunit alpha-1. A/J mice had an increase in proteins related to energy flux and oxidative stress. Conclusion This could be a possible explanation for the high susceptibility of these mice to the effects of F, since the exposure also induces oxidative stress.
Descritores: Fluoretos/toxicidade
Fluorose Dentária/genética
Predisposição Genética para Doença
Fígado/efeitos dos fármacos
Fígado/metabolismo
Proteínas/análise
Proteoma/efeitos dos fármacos
-Fluoretos/análise
Fluoretos/metabolismo
Expressão Gênica
Espectrometria de Massas/métodos
Camundongos da Linhagem 129
Camundongos Endogâmicos A
Estresse Oxidativo/efeitos dos fármacos
Domínios e Motivos de Interação entre Proteínas
Proteínas/efeitos dos fármacos
Proteínas/genética
Proteômica/métodos
Valores de Referência
Fatores de Tempo
Limites: Animais
Masculino
Camundongos
Responsável: BR1.1 - BIREME


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Id: lil-753056
Autor: Aquino, B; Stefanello, AA; Oliveira, MAS; Pedrosa, FO; Souza, EM; Monteiro, RA; Chubatsu, LS.
Título: Effect of point mutations on Herbaspirillum seropedicae NifA activity
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;48(8):683-690, 08/2015. tab, graf.
Idioma: en.
Resumo: NifA is the transcriptional activator of the nif genes in Proteobacteria. It is usually regulated by nitrogen and oxygen, allowing biological nitrogen fixation to occur under appropriate conditions. NifA proteins have a typical three-domain structure, including a regulatory N-terminal GAF domain, which is involved in control by fixed nitrogen and not strictly required for activity, a catalytic AAA+ central domain, which catalyzes open complex formation, and a C-terminal domain involved in DNA-binding. In Herbaspirillum seropedicae, a β-proteobacterium capable of colonizing Graminae of agricultural importance, NifA regulation by ammonium involves its N-terminal GAF domain and the signal transduction protein GlnK. When the GAF domain is removed, the protein can still activate nif genes transcription; however, ammonium regulation is lost. In this work, we generated eight constructs resulting in point mutations in H. seropedicae NifA and analyzed their effect on nifH transcription in Escherichia coli and H. seropedicae. Mutations K22V, T160E, M161V, L172R, and A215D resulted in inactive proteins. Mutations Q216I and S220I produced partially active proteins with activity control similar to wild-type NifA. However, mutation G25E, located in the GAF domain, resulted in an active protein that did not require GlnK for activity and was partially sensitive to ammonium. This suggested that G25E may affect the negative interaction between the N-terminal GAF domain and the catalytic central domain under high ammonium concentrations, thus rendering the protein constitutively active, or that G25E could lead to a conformational change comparable with that when GlnK interacts with the GAF domain.
Descritores: Proteínas de Bactérias/genética
Escherichia coli/genética
Herbaspirillum/genética
Fatores de Transcrição/genética
-Proteínas de Bactérias/química
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Herbaspirillum/metabolismo
Fixação de Nitrogênio/genética
Mutação Puntual
Domínios e Motivos de Interação entre Proteínas
Fatores de Transcrição/química
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-594210
Autor: Souza, Diorge Paulo de.
Título: Estudos estruturais e de interações proteína-proteína envolvendo componentes de um sistema de secreção do tipo IV de Xanthomonas axonopodis pv. citri / Structural and protein-protein interaction studies of type IV secretion system components from Xanthomonas axonopodis pv. citri.
Fonte: São Paulo; s.n; 2010. 227 p. ilus, tab, graf.
Idioma: pt.
Tese: Apresentada a Universidade de São Paulo. Instituto de Química para obtenção do grau de Doutor.
Resumo: Xanthomonas axonopodis pv. citri (Xac) é o causador do cancro de plantas cítricas. Entre os potenciais fatores de virulência codificados por Xac, está o Sistema de Secreção do Tipo IV (T4SS), um grande complexo multiprotéico que atravessa o periplasma e as membranas interna e externa de bactérias Gram-negativas. O T4SS está envolvido com secreção de proteínas e/ou DNA para o meio extracelular ou diretamente no interior da célula do hospedeiro. Este Sistema requer tipicamente 12 proteínas para realizar suas funções: VirB1-VirB11 e VirD4. O T4SS codificado pelo cromossomo de Xac está aparentemente incompleto, devido a não codificar nenhuma proteína com similaridade de seqüência a VirB7. Os objetivos deste trabalho são estudar a estrutura, função e interações das proteínas do T4SS de Xanthomonas. Foram clonados 23 genes que codificam proteínas ou domínios relacionados ao T4SS, e os polipeptídeos foram produzidos de forma recombinante em E. coli. Treze deles foram purificados e submetidos a estudos estruturais, espectroscópicos e de interações proteína-proteína. A estrutura em solução de Xac262224-139 foi resolvida, apresentando uma região N-terminal desenovelada de aproximadamente 30 resíduos e um domínio globular. Este polipeptídeo oligomeriza em troca química rápida na escala de tempo de RMN e o seu N-terminal desenovelado reconhece o domínio C-terminal de VirB9 (VirB9154-255) em troca lenta. Análise de RMN demonstrou que VirB9154-255 possui uma estrutura flexível em solução, sofrendo uma marcante mudança conformacional na presença de Xac262224-139. Ambas proteínas se tornam rígidas após a interação. Xac2622 é o equivalente a VirB7 em Xanthomonas, baseado na localização do seu gene no lócus do T4SS, localização subcelular predita do polipeptídeo codificado e sua interação com VirB9...

Xanthomonas axonopodis pv. citri (Xac) is a gram-negative bacterial phytopathogen that infects citrus. One possible virulence determinant is a chromosomally encoded Type IV Secretion System (T4SS), a multiprotein complex that spans the bacterial periplasm and both inner and outer membranes. The T4SS is used by some bacteria to secrete proteins and/or DNA to the extracellular milieu or the host interior. The model T4SS from Agrobacterium tumefaciens is made up of twelve structural proteins: VirB1-VirB11 and VirD4. The Xanthomonas T4SS is apparently incomplete because of the lack of a polypeptide with sequence similarity to VirB7. The aim of this project is the study of structure-function relationships in the Xanthomonas T4SS. Twenty-three T4SS protein-coding genes, including full-length proteins or domains, were cloned and the proteins were produced in different E. coli strains. Thirteen polypeptides were purified and some of them were submitted to structural, spectroscopic and protein-protein interaction studies. We used NMR to solve the solution structure of Xac262224-139 which consists of an unfolded N-terminal segment of ~30 residues followed by a globular domain. Xac262224-139 oligomerizes in fast exchange at the NMR time scale and interacts via its unfolded N-terminus with the VirB9 C-terminus (VirB9154-255) in slow exchange. NMR analysis showed that VirB9154-255 has a flexible structure in solution. However, this polypeptide undergoes a significant conformational modification in the presence of Xac2622,24-139 and both proteins become rigid upon interaction. Xac2622 is the Xanthomonas VirB7, based on the chromosomal localization of its gene, predicted subcellular localization and protein interaction analysis. But surprisingly, unlike other VirB7 proteins, Xac2622 has an extra C-terminal folded domain whose topology and structure are strikingly similar to that of periplasmic domains found in outer membrane proteins of many bacterial Secretion Systems...
Descritores: Infecções por Bactérias Gram-Negativas/patologia
Xanthomonas axonopodis/química
-Cristalografia por Raios X
Espectroscopia de Ressonância Magnética
Domínios e Motivos de Interação entre Proteínas
Taxa Secretória/fisiologia
Tipo de Publ: Estudo de Avaliação
Responsável: BR40.1 - DBD - Divisão de Biblioteca e Documentacão do Conjunto das Químicas
BR40.1; T574.19245, S729e. 24025



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