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izvor podataka: crosbi

Chloroplast complex immunophilin CYP38 as a target for RNAi silencing (CROSBI ID 679510)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija

Fulgosi, Hrvoje ; Vojta, Lea Chloroplast complex immunophilin CYP38 as a target for RNAi silencing // Program of the 3rd iPlanta Conference. 2019. str. 3-3

Podaci o odgovornosti

Fulgosi, Hrvoje ; Vojta, Lea

engleski

Chloroplast complex immunophilin CYP38 as a target for RNAi silencing

Immunophilins are ubiquitous proteins found in all phyla from prokaryotes to eukaryotes. They are involved in cellular regulatory pathways, signalling, protein folding, and protein trafficking (Marks 1996 ; He et al. 2004 ; Romano et al. 2005). Initially defined in 1989, when it was reported that previously discovered cyclophilin and peptidyl-prolyl cis-trans isomerase are identical proteins (Takahashi et al. 2003 ; Fischer et al. 1989), immunophilins comprise three functionally related families: cyclophilins (CYP), FK506/rapamycin-binding proteins (FKBP), and parvulins. Immunophilins bind immunosuppressive drugs cyclosporine A and FK506/rapamycin but are not directly involved in immune responses in mammals. A striking feature of the immunophilins found in chloroplasts of vascular plants is their particular abundance in the thylakoid lumen, rather than in the stroma or in the intermembrane space of the envelope. Complex immunofilin from thylakoid lumen, AtCYP38, with many proposed functions, also acts as a regulator of a thylakoid-associated phosphatase. This PP2A-like phosphatase is postulated to dephosphorylate both CP43 antenna and PSII core proteins. The AtCYP38-knock-out plants grown under light–dark regime exhibit dramatic retardation of growth, small leaves, and poor seedling survival. The observed stunned phenotype is however abolished in conditions of continuous illumination. The AtCYP38 knock-outs were found highly susceptible to photodamage, accompanied with a reduced PSII activity and impaired fine-tuning of the oxygen-evolving complexes. In our future studies of the CYP38 we will employ RNAi technology to address its possible additional functions and interactions.

FK506/rapamycin-binding proteins (FKBP) ; parvulins ; thylakoid lumen

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Podaci o prilogu

3-3.

2019.

objavljeno

Podaci o matičnoj publikaciji

Program of the 3rd iPlanta Conference

Podaci o skupu

3rd iPlanta Conference What Future for RNAi-Based Products: RNAi Modified Plants or Spray Products

predavanje

27.02.2019-01.03.2019

Oeiras, Portugal

Povezanost rada

Biologija