About: Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Gradual heating of green leaves up to non-physiological temperatures is often used to estimate thermal stability of photosynthetic apparatus. However, a complete sequence of heat-induced disassembly and denaturation of chlorophyll-containing protein complexes (CPCs) has not been reported yet. In this work, we heated (1 °C min-1) barley leaves to temperatures selected according to the changes in the chlorophyll fluorescence temperature curve (FTC) and we analyzed CPC stability by two-dimensional native Deriphat/SDS-PAGE. The first distinct change in both structure and function of photosystem II (PSII) appeared at 40-50 °C. PSII core (CCII) dimers began to dissociate monomers, which was accompanied by a decrease in PSII photochemistry and reflected in FTC as the first fluorescence increase. Further changes in CPCs appeared at 57-60 °C, when FTC increases to its second maximum. Photosystem I (PSI) cores (CCI) partially dissociated from light-harvesting complexes of PSI (LHCI) and formed aggregates. Gradual heating of green leaves up to non-physiological temperatures is often used to estimate thermal stability of photosynthetic apparatus. However, a complete sequence of heat-induced disassembly and denaturation of chlorophyll-containing protein complexes (CPCs) has not been reported yet. In this work, we heated (1 °C min-1) barley leaves to temperatures selected according to the changes in the chlorophyll fluorescence temperature curve (FTC) and we analyzed CPC stability by two-dimensional native Deriphat/SDS-PAGE. The first distinct change in both structure and function of photosystem II (PSII) appeared at 40-50 °C. PSII core (CCII) dimers began to dissociate monomers, which was accompanied by a decrease in PSII photochemistry and reflected in FTC as the first fluorescence increase. Further changes in CPCs appeared at 57-60 °C, when FTC increases to its second maximum. Photosystem I (PSI) cores (CCI) partially dissociated from light-harvesting complexes of PSI (LHCI) and formed aggregates. (en)
Title	Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo (en)
skos:prefLabel	Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo (en)
skos:notation	RIV/61989592:15310/10:10212225!RIV11-MSM-15310___
http://linked.open...avai/riv/aktivita	S Z
http://linked.open...avai/riv/aktivity	S, Z(AV0Z50200510), Z(MSM6198959215)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2011
http://linked.open...aciTvurceVysledku	Krchňák, Pavel Ilík, Petr Lípová, Lenka
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	261316
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/10:10212225
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	native electrophoresis; high temperature; heat denaturation; chlorophyll fluorescence temperature curve, disassembly; chlorophyll-containing protein complexes (en)
http://linked.open.../riv/klicoveSlovo	native electrophoresis high temperature disassembly chlorophyll fluorescence temperature curve chlorophyll-containing protein complexes heat denaturation
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[1A2212819C0A]
http://linked.open...i/riv/nazevZdroje	Biochimica et Biphysica Acta - Bioenergetics
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...UplatneniVysledku	2010
http://linked.open...v/svazekPeriodika	1797
http://linked.open...iv/tvurceVysledku	Ilík, Petr Komenda, Josef Krchňák, Pavel Lípová, Lenka
http://linked.open...ain/vavai/riv/wos	000272856900008
http://linked.open...n/vavai/riv/zamer	Microorganisms in Research and Biotechnology Variabilita složek a interakcí v rostlinném patosystému a vliv faktorů prostředí na jejich projev
issn	0005-2728
number of pages	8 (xsd:int)
http://localhost/t...ganizacniJednotka	15310

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