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1.
Epigenetics Chromatin ; 11(1): 43, 2018 08 01.
Artigo em Inglês | MEDLINE | ID: mdl-30068355

RESUMO

BACKGROUND: Linker histones establish and maintain higher-order chromatin structure. Eleven linker histone subtypes have been reported in mammals. HILS1 is a spermatid-specific linker histone, and its expression overlaps with the histone-protamine exchange process during mammalian spermiogenesis. However, the role of HILS1 in spermatid chromatin remodeling is largely unknown. RESULTS: In this study, we demonstrate using circular dichroism spectroscopy that HILS1 is a poor condenser of DNA and chromatin compared to somatic linker histone H1d. Genome-wide occupancy study in elongating/condensing spermatids revealed the preferential binding of HILS1 to the LINE-1 (L1) elements within the intergenic and intronic regions of rat spermatid genome. We observed specific enrichment of the histone PTMs like H3K9me3, H4K20me3 and H4 acetylation marks (H4K5ac and H4K12ac) in the HILS1-bound chromatin complex, whereas H3K4me3 and H3K27me3 marks were absent. CONCLUSIONS: HILS1 possesses significantly lower α-helicity compared to other linker histones such as H1t and H1d. Interestingly, in contrast to the somatic histone variant H1d, HILS1 is a poor condenser of chromatin which demonstrate the idea that this particular linker histone variant may have distinct role in histone to protamine replacement. Based on HILS1 ChIP-seq analysis of elongating/condensing spermatids, we speculate that HILS1 may provide a platform for the structural transitions and forms the higher-order chromatin structures encompassing LINE-1 elements during spermiogenesis.


Assuntos
Cromatina/genética , Proteínas de Ligação a DNA/metabolismo , DNA/genética , Espermátides/metabolismo , Animais , Proteínas de Ligação a DNA/química , Histonas/metabolismo , Elementos Nucleotídeos Longos e Dispersos , Masculino , Processamento de Proteína Pós-Traducional , Estrutura Secundária de Proteína , Ratos , Espermátides/química
2.
PLoS One ; 9(6): e98589, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24893006

RESUMO

Veterinary nosocomial infections caused by antibiotic resistant bacteria cause increased morbidity, higher cost and length of treatment and increased zoonotic risk because of the difficulty in treating them. In this study, an individual-based model was developed to investigate the effects of movements of canine patients among ten areas (transmission points) within a veterinary teaching hospital, and the effects of these movements on transmission of antibiotic susceptible and resistant pathogens. The model simulates contamination of transmission points, healthcare workers, and patients as well as the effects of decontamination of transmission points, disinfection of healthcare workers, and antibiotic treatments of canine patients. The model was parameterized using data obtained from hospital records, information obtained by interviews with hospital staff, and the published literature. The model suggested that transmission resulting from contact with healthcare workers was common, and that certain transmission points (housing wards, diagnostics room, and the intensive care unit) presented higher risk for transmission than others (lobby and surgery). Sensitivity analyses using a range of parameter values demonstrated that the risk of acquisition of colonization by resistant pathogens decreased with shorter patient hospital stays (P<0.0001), more frequent decontamination of transmission points and disinfection of healthcare workers (P<0.0001) and better compliance of healthcare workers with hygiene practices (P<0.0001). More frequent decontamination of heavily trafficked transmission points was especially effective at reducing transmission of the model pathogen.


Assuntos
Infecções Bacterianas/transmissão , Hospitais Veterinários/estatística & dados numéricos , Hospitais de Ensino/estatística & dados numéricos , Animais , Antibacterianos/uso terapêutico , Infecções Bacterianas/tratamento farmacológico , Infecção Hospitalar/transmissão , Farmacorresistência Bacteriana
3.
J Agric Food Chem ; 59(11): 6256-62, 2011 Jun 08.
Artigo em Inglês | MEDLINE | ID: mdl-21528916

RESUMO

Proteases have several applications in the food industry. We report the immobilization of procerain B, a novel cysteine protease, on glutaraldehyde-activated chitosan beads through covalent attachment. Glutaraldehyde not only serves as a cross-linking agent but also links the procerain B on the surface of bead through primary amine group (either lysine side chain or N-terminal) by Schiff base linkage. Immobilized procerain B was characterized for optimum functional range and stability with respect to pH and temperature. The chitosan-immobilized procerain B has broad pH and thermal optima. The effects of substrate concentration and reusability of immobilized beads were also studied. It showed nearly 50% activity until the 10th use.


Assuntos
Calotropis/enzimologia , Cisteína Endopeptidases/química , Glutaral/química , Proteínas de Plantas/química , Calotropis/química , Quitosana/química , Estabilidade Enzimática , Enzimas Imobilizadas/química , Concentração de Íons de Hidrogênio , Cinética , Temperatura
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