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	Provedor de dados BJMBR (2) Biol. Res. (1) Autor Bastos,C.M.V. (1) Bolean,M. (1) Carreira,A.C.O. (1) Ciancaglini,P. (1) HENRÍQUEZ,DANIEL R (1) Leitão,D.P.S. (1) NAVARRO,CLAUDIO A (1) PICHUANTES,SERGIO E (1) PRADEÑAS,GONZALO A (1) Paulino,T.P. (1) PÉREZ,JOSÉ M (1) Spadaro,A.C.C. (1) Thedei Jr.,G. (1) Verjovski-Almeida,S. (1) VÁSQUEZ,CLAUDIO C (1) Mais... Palavra-chave P-type ATPase (3) CadA (1) Cadmium (1) Catalytic site (1) Cell permeabilization (1) F-type ATPase (1) Lead (1) Phosphorylation site mutant (1) Saccharomyces cerevisiae (1) Streptococcus mutans (1) Toluene permeabilization (1) Yeast expression system (1) Zinc (1) ZntA (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Journal article (1) Ano 2008 (1) 2007 (1) 2006 (1) País Brazil (2) Chile (1) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Geobacillus stearothermophilus LV cadA gene mediates resistance to cadmium, lead and zinc in zntA mutants of Salmonella entérica serovar Typhimurium Biol. Res. PÉREZ,JOSÉ M; PRADEÑAS,GONZALO A; NAVARRO,CLAUDIO A; HENRÍQUEZ,DANIEL R; PICHUANTES,SERGIO E; VÁSQUEZ,CLAUDIO C. Salmonella entérica serovar Typhimurium cells expressing the cadA gene of Geobacillus stearothermophilus LV exhibit a hypersensitive phenotype to cadmium chloride. Deletion of the ORF STM3576 from the Salmonella genome resulted in cadmium, lead and zinc sensitivity, confirming that this ORF is a homologue of the zntA gene. The observed sensitivity was reverted upon expression of the G. stearothermophilus LV cadA gene. These results indicate that the cadA gene product is involved in Cd, Pb and Zn resistance as a classical P-type ATPase and strongly suggest that the observed hypersensitive phenotype to these metals can be related to the function of the host ·zntA gene product Tipo: Journal article Palavras-chave: CadA; Cadmium; Lead; P-type ATPase; Zinc; ZntA. Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000500009 Probing the SERCA1a sarcoplasmic reticulum Ca2+-ATPase phosphorylation-site mutant D351E with inorganic phosphate BJMBR Carreira,A.C.O.; Bastos,C.M.V.; Verjovski-Almeida,S.. The expression of sarcoplasmic reticulum SERCA1a Ca2+-ATPase wild-type and D351E mutants was optimized in yeast under the control of a galactose promoter. Fully active wild-type enzyme was recovered in yeast microsomal membrane fractions in sufficient amounts to permit a rapid and practical assay of ATP hydrolysis and phosphoenzyme formation from ATP or Pi. Mutant and wild-type Ca2+-ATPase were assayed for phosphorylation by Pi under conditions that are known to facilitate this reaction in the wild-type enzyme, including pH 6.0 or 7.0 at 25ºC in the presence of dimethylsulfoxide. Although glutamyl (E) and aspartyl (D) residue side chains differ by only one methylene group, no phosphoenzyme could be detected in the D351E mutant, even upon the addition of... Tipo: Info:eu-repo/semantics/article Palavras-chave: Phosphorylation site mutant; Catalytic site; Yeast expression system; Saccharomyces cerevisiae; P-type ATPase. Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001000004 Toluene permeabilization differentially affects F- and P-type ATPase activities present in the plasma membrane of Streptococcus mutans BJMBR Thedei Jr.,G.; Leitão,D.P.S.; Bolean,M.; Paulino,T.P.; Spadaro,A.C.C.; Ciancaglini,P.. Streptococcus mutans membrane-bound P- and F-type ATPases are responsible for H+ extrusion from the cytoplasm thus keeping intracellular pH appropriate for cell metabolism. Toluene-permeabilized bacterial cells have long been used to study total membrane-bound ATPase activity, and to compare the properties of ATPase in situ with those in membrane-rich fractions. The aim of the present research was to determine if toluene permeabilization can significantly modify the activity of membrane-bound ATPase of both F-type and P-type. ATPase activity was assayed discontinuously by measuring phosphate release from ATP as substrate. Treatment of S. mutans membrane fractions with toluene reduced total ATPase activity by approximately 80% and did not allow... Tipo: Info:eu-repo/semantics/article Palavras-chave: Cell permeabilization; F-type ATPase; P-type ATPase; Toluene permeabilization; Streptococcus mutans. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008001200002 Registros recuperados: 3 Primeira ... 1 ... Última

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