Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00362744" target="_blank" >RIV/61388971:_____/11:00362744 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1074/jbc.M110.207944" target="_blank" >http://dx.doi.org/10.1074/jbc.M110.207944</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M110.207944" target="_blank" >10.1074/jbc.M110.207944</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe

Popis výsledku v původním jazyce

Using the cyanobacterium Synechocystis sp. PCC 6803, we describe here the isolation of the CP47 and CP43 subunits, which, during biogenesis, attach to a reaction center assembly complex containing D1, D2, and cytochrome b559, with CP47 binding first. Absorption spectroscopy and pigment analyses revealed that both CP47-His and CP43-His bind chlorophyll a and âcarotene. A comparison of the low temperature absorption and fluorescence spectra in theQY region for CP47-His and CP43-His with those for CP47 andCP43 isolated by fragmentation of spinach PSII core complexes confirmed that the spectroscopic properties are similar but not identical. Immunoblotting and mass spectrometry revealed the co-purification of PsbH, PsbL, and PsbT with CP47-His and of PsbKand Psb30/Ycf12 with CP43-His. Overall, our data support the view that CP47 and CP43 form preassembled pigment-protein complexes in vivo before their incorporation into the PSII complex

Název v anglickém jazyce

Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe

Popis výsledku anglicky

Using the cyanobacterium Synechocystis sp. PCC 6803, we describe here the isolation of the CP47 and CP43 subunits, which, during biogenesis, attach to a reaction center assembly complex containing D1, D2, and cytochrome b559, with CP47 binding first. Absorption spectroscopy and pigment analyses revealed that both CP47-His and CP43-His bind chlorophyll a and âcarotene. A comparison of the low temperature absorption and fluorescence spectra in theQY region for CP47-His and CP43-His with those for CP47 andCP43 isolated by fragmentation of spinach PSII core complexes confirmed that the spectroscopic properties are similar but not identical. Immunoblotting and mass spectrometry revealed the co-purification of PsbH, PsbL, and PsbT with CP47-His and of PsbKand Psb30/Ycf12 with CP43-His. Overall, our data support the view that CP47 and CP43 form preassembled pigment-protein complexes in vivo before their incorporation into the PSII complex

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/IAA400200801" target="_blank" >IAA400200801: Proteázy FtsH a jejich funkce v sinici Synechocystis PCC 6803</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

286

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

14812-14819

Kód UT WoS článku

000289788300011

EID výsledku v databázi Scopus

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