Proteázy Deg chrání sinici Synechocystis PCC 6803 běhen teplotního a světelného stresu ale nejsou nezbytné k odstranění poškozené bílkoviny D1 během opravy fotosystému II

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00082608" target="_blank" >RIV/61388971:_____/06:00082608 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

The Deg proteases protect Synechocystis sp. PCC 6803 during heat and light stresses but are not essential for removal of damaged D1 protein during the Photosystem two repair cycle

Popis výsledku v původním jazyce

Members of the DegP/HtrA (or Deg) family of proteases play an important role in the proteolysis of misfolded and damaged proteins. As yet, their physiological role in oxygenic photosynthetic organisms is unclear, although it has been widely speculated that they participate in the degradation of the photodamaged D1 subunit in the photosystem two complex (PSII) repair cycle, which is needed to maintain PSII activity in both cyanobacteria and chloroplasts. In this work, we have now been able to demonstrateunambiguously, using a triple deg mutant created in the wild type strain of Synechocystis 6803, that although the Deg proteases are needed for photoprotection of Synechocystis sp. PCC 6803, they do not play an essential role in D1 turnover and PSII repair in vivo

Název v anglickém jazyce

The Deg proteases protect Synechocystis sp. PCC 6803 during heat and light stresses but are not essential for removal of damaged D1 protein during the Photosystem two repair cycle

Popis výsledku anglicky

Members of the DegP/HtrA (or Deg) family of proteases play an important role in the proteolysis of misfolded and damaged proteins. As yet, their physiological role in oxygenic photosynthetic organisms is unclear, although it has been widely speculated that they participate in the degradation of the photodamaged D1 subunit in the photosystem two complex (PSII) repair cycle, which is needed to maintain PSII activity in both cyanobacteria and chloroplasts. In this work, we have now been able to demonstrateunambiguously, using a triple deg mutant created in the wild type strain of Synechocystis 6803, that although the Deg proteases are needed for photoprotection of Synechocystis sp. PCC 6803, they do not play an essential role in D1 turnover and PSII repair in vivo

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2006

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

281

Číslo periodika v rámci svazku

41

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

30347-30355

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—