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Statements

Subject Item
n2:RIV%2F67985823%3A_____%2F12%3A00376829%21RIV13-GA0-67985823
rdf:type
skos:Concept n19:Vysledek
dcterms:description
In this work, we investigated in detail the interaction between Saccharomyces cerevisiae Nth1 and 14-3-3 protein isoforms Bmh1 and Bmh2. We determined four residues that are phosphorylated by PKA within the disordered N-terminal segment of Nth1. Sedimentation analysis and enzyme kinetics measurements show that both yeast 14-3-3 isoforms form a stable complex with phosphorylated NTH1 and significantly enhance its enzyme activity. Site-directed mutagenesis was used to decipher the importance of found phosphorylation sites for Nth1 activation. These experiments suggest that Ser60 and Ser83 are essential sites for PKA-dependent and 14-3-3-mediated activation of Nth1. The phosphorylation of either of these sites is sufficient for full 14-3-3-dependent activation of Nth1 In this work, we investigated in detail the interaction between Saccharomyces cerevisiae Nth1 and 14-3-3 protein isoforms Bmh1 and Bmh2. We determined four residues that are phosphorylated by PKA within the disordered N-terminal segment of Nth1. Sedimentation analysis and enzyme kinetics measurements show that both yeast 14-3-3 isoforms form a stable complex with phosphorylated NTH1 and significantly enhance its enzyme activity. Site-directed mutagenesis was used to decipher the importance of found phosphorylation sites for Nth1 activation. These experiments suggest that Ser60 and Ser83 are essential sites for PKA-dependent and 14-3-3-mediated activation of Nth1. The phosphorylation of either of these sites is sufficient for full 14-3-3-dependent activation of Nth1
dcterms:title
Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1 Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1
skos:prefLabel
Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1 Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1
skos:notation
RIV/67985823:_____/12:00376829!RIV13-GA0-67985823
n19:predkladatel
n20:ico%3A67985823
n3:aktivita
n9:Z n9:I n9:S n9:P
n3:aktivity
I, P(GAP207/11/0455), P(IAA500110801), S, Z(AV0Z50110509), Z(AV0Z50200510), Z(MSM0021620857)
n3:cisloPeriodika
3
n3:dodaniDat
n14:2013
n3:domaciTvurceVysledku
n13:2152037 n13:2715201 n13:7091184 n13:9978194 n13:6869203 n13:2968797
n3:druhVysledku
n5:J
n3:duvernostUdaju
n8:S
n3:entitaPredkladatele
n11:predkladatel
n3:idSjednocenehoVysledku
166009
n3:idVysledku
RIV/67985823:_____/12:00376829
n3:jazykVysledku
n17:eng
n3:klicovaSlova
14-3-3 protein; Bmh; neutral trehalase (Nth1); enzymatic activity; phosphorylation; Saccharomyces cerevisiae
n3:klicoveSlovo
n6:Bmh n6:neutral%20trehalase%20%28Nth1%29 n6:Saccharomyces%20cerevisiae n6:phosphorylation n6:enzymatic%20activity n6:14-3-3%20protein
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[5BBAABD80D4C]
n3:nazevZdroje
Biochemical Journal
n3:obor
n16:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
8
n3:projekt
n18:IAA500110801 n18:GAP207%2F11%2F0455
n3:rokUplatneniVysledku
n14:2012
n3:svazekPeriodika
443
n3:tvurceVysledku
Veisová, Dana Vácha, Petr Řežábková, Lenka Obšil, T. Šulc, Miroslav Obšilová, Veronika Sychrová, Hana Macáková, Eva
n3:wos
000303944200008
n3:zamer
n7:MSM0021620857 n7:AV0Z50110509 n7:AV0Z50200510
s:issn
0264-6021
s:numberOfPages
8
n10:doi
10.1042/BJ20111615