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Revealing phosphoproteins playing role in tobacco pollen activated in vitro
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SYSNO ASEP 0384621 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Revealing phosphoproteins playing role in tobacco pollen activated in vitro Tvůrce(i) Fíla, Jan (UEB-Q) RID, ORCID
Matros, A. (DE)
Radau, S. (DE)
Zahedi, R. P. (DE)
Čapková, Věra (UEB-Q) RID
Mock, H. P. (DE)
Honys, David (UEB-Q) RID, ORCIDZdroj.dok. Proteomics. - : Wiley - ISSN 1615-9853
Roč. 12, č. 21 (2012), s. 3229-3250Poč.str. 22 s. Jazyk dok. eng - angličtina Země vyd. DE - Německo Klíč. slova Male gametophyte ; Metal oxide affinity chromatography ; Nicotiana tabacum Vědní obor RIV ED - Fyziologie CEP GAP501/11/1462 GA ČR - Grantová agentura ČR GAP305/12/2611 GA ČR - Grantová agentura ČR CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000310564100012 DOI 10.1002/pmic.201100318 Anotace The transition between the quiescent mature and the metabolically active germinating pollen grain most probably involves changes in protein phosphorylation status, since phosphorylation has been implicated in the regulation of many cellular processes. Given that, only a minor proportion of cellular proteins are phosphorylated at any one time, and that phosphorylated and nonphosphorylated forms of many proteins can co-exist within a cell, the identification of phosphoproteins requires some prior enrichment from a crude protein extract. Here, we have used metal oxide/hydroxide affinity chromatography (MOAC) based on an aluminum hydroxide matrix for this purpose, and have generated a population of phosphoprotein candidates from both mature and in vitro activated tobacco pollen grains. Both electrophoretic and nonelectrophoretic methods, allied to MS, were applied to these extracts to identify a set of 139 phosphoprotein candidates. In vitro phosphorylation was also used to validate the spectrum of phosphoprotein candidates obtained by the MOAC phosphoprotein enrichment. Since only one phosphorylation site was detected by the above approach, titanium dioxide phosphopeptide enrichment of trypsinized mature pollen crude extract was performed as well. It resulted in a detection of additional 51 phosphorylation sites giving a total of 52 identified phosphosites in this set of 139 phosphoprotein candidates. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2013
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