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Statements

Subject Item
n2:RIV%2F61389030%3A_____%2F03%3A56033063%21RIV%2F2004%2FAV0%2FA56004%2FN
rdf:type
skos:Concept n9:Vysledek
dcterms:description
Phospholipase D (PLD) forms the major family of phospholipases that was first discovered and cloned in plants. In this report we have shown, for the first time, that C2 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using matrix-assisted laser desorption/ionization time of flight mass spectrometry of tryptic in-gel digests, the BoPLD1,2 isoform was identified. Comparing the spectra of the proteins obtained from the plasma membrane fractions treated and non-treated with acid phosphatase, three peptides differing in the mass of the phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which possess five potential Ser/Thr phosphorylation sites. Our findings suggest that a phosphorylation/dephosphorylation Phospholipase D (PLD) forms the major family of phospholipases that was first discovered and cloned in plants. In this report we have shown, for the first time, that C2 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using matrix-assisted laser desorption/ionization time of flight mass spectrometry of tryptic in-gel digests, the BoPLD1,2 isoform was identified. Comparing the spectra of the proteins obtained from the plasma membrane fractions treated and non-treated with acid phosphatase, three peptides differing in the mass of the phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which possess five potential Ser/Thr phosphorylation sites. Our findings suggest that a phosphorylation/dephosphorylation
dcterms:title
Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation . Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation .
skos:prefLabel
Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation . Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation .
skos:notation
RIV/61389030:_____/03:56033063!RIV/2004/AV0/A56004/N
n4:strany
50;54
n4:aktivita
n7:P n7:Z
n4:aktivity
P(LN00A081), Z(AV0Z5038910), Z(MSM 223300006)
n4:cisloPeriodika
1
n4:dodaniDat
n14:2004
n4:domaciTvurceVysledku
n12:9481923
n4:druhVysledku
n8:J
n4:duvernostUdaju
n13:S
n4:entitaPredkladatele
n17:predkladatel
n4:idSjednocenehoVysledku
621026
n4:idVysledku
RIV/61389030:_____/03:56033063
n4:jazykVysledku
n18:eng
n4:klicovaSlova
Phospholipase D; Phosphorylation; Cytoskeleton
n4:klicoveSlovo
n10:Phospholipase%20D n10:Phosphorylation n10:Cytoskeleton
n4:kodStatuVydavatele
NL - Nizozemsko
n4:kontrolniKodProRIV
[D02F60A5E32B]
n4:nazevZdroje
FEBS Letters
n4:obor
n16:CE
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
6
n4:pocetUcastnikuAkce
0
n4:pocetZahranicnichUcastnikuAkce
0
n4:projekt
n11:LN00A081
n4:rokUplatneniVysledku
n14:2003
n4:svazekPeriodika
554
n4:tvurceVysledku
Hynek, R. Valentová, O. Martinec, Jan Novotná, Z. Linek, J. Potocký, M.
n4:zamer
n5:AV0Z5038910 n5:MSM%20223300006
s:issn
0014-5793
s:numberOfPages
5