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| da-Silva,A.M.; Zapella,P.D.A.; Andrioli,L.P.M.; Campanhã,R.B.; Fiorini,L.C.; Etchebehere,L.C.; da-Costa-Maia,J.C.; Terenzi,H.F.. |
| Preference for specific protein substrates together with differential sensitivity to activators and inhibitors has allowed classification of serine/threonine protein phosphatases (PPs) into four major types designated types 1, 2A, 2B and 2C (PP1, PP2A, PP2B and PP2C, respectively). Comparison of sequences within their catalytic domains has indicated that PP1, PP2A and PP2B are members of the same gene family named PPP. On the other hand, the type 2C enzyme does not share sequence homology with the PPP members and thus represents another gene family, known as PPM. In this report we briefly summarize some of our studies about the role of serine/threonine phosphatases in growth and differentiation of three different eukaryotic models: Blastocladiella... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Protein phosphatases; Blastocladiella emersonii; Neurospora crassa; Dictyostelium discoideum. |
| Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000700006 |
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| Morales,A.C.; Nozawa,S.R.; Thedei Jr.,G.; Maccheroni Jr.,W.; Rossi,A.. |
| A constitutive alkaline phosphatase was purified to apparent homogeneity as determined by polyacrylamide gel electrophoresis from mycelia of the wild strain 74A of the mold Neurospora crassa, after growth on acetate and in the presence of saturating amounts of inorganic phosphate (Pi) for 72 h at 30ºC. The molecular mass was 58 kDa and 56 kDa as determined by exclusion chromatography and SDS-PAGE, respectively. This monomeric enzyme shows an apparent optimum pH ranging from 9.5 to 10.5 and Michaelis kinetics for the hydrolysis of p-nitrophenyl phosphate (the Km and Hill coefficient values were 0.35 mM and 1.01, respectively), alpha-naphthyl phosphate (the Km and Hill coefficient values were 0.44 mM and 0.97, respectively), ß-glycerol phosphate (the Km and... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Neurospora crassa; Fungi; Alkaline phosphatase; L-histidinol-Pi phosphatase. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000800006 |
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| Nozawa,Sérgio R.; Thedei Jr.,Geraldo; Crott,Luciana S.P.; Barbosa,José E.; Rossi,Antonio. |
| In order to investigate further the adaptive response of moulds to ambient pH, we have measured by ELISA the pho-2-encoded Pi-repressible alkaline phosphatase synthesised by Neurospora crassa. We showed that the 74A and pho-2A strains of this mould secrete similar amounts of the pho-2-encoded enzyme irrespective of ambient pH, when both the preg and pgov genes are not functional, i.e., in strains nuc-2+ growing under Pi-starvation. This suggests that pho-2, which is responsive to Pi starvation via the action of genes nuc-2, preg, pgov and nuc-1, is not a gene responsive to ambient pH and that the differential glycosylation observed for the Pi-repressible alkaline phosphatase retained by the mycelium at pH 5.6 or secreted into the growth medium at pH 8.0 is... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alkaline phosphatase; Ambient pH; Enzyme secretion; Neurospora crassa; Pi sensing. |
| Ano: 2002 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000100018 |
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