Pregled bibliografske jedinice broj: 368557
TLP40 is involved in state II transitions
TLP40 is involved in state II transitions // Book of Abstracts of the HDBMB 2008, Congress of the Croatian Society of Biochemistry and Molecular Biology with International Participation / Strelec, Ivica ; Glavaš-Obrovac, Ljubica (ur.). - Osijek: Croatian Society of Biochemistry and Molecular Biology, 2008. 137.
Osijek, Hrvatska, 2008. (poster, međunarodna recenzija, sažetak, znanstveni)
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Naslov
TLP40 is involved in state II transitions
Autori
Tomašić, Ana ; Jurić, Snježana ; Prebeg, Tatjana ; Horvat, Lucija ; Lepeduš, Hrvoje ; Puthiyaveetil, Sujith ; Allen, John F. ; Fulgosi, Hrvoje
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Book of Abstracts of the HDBMB 2008, Congress of the Croatian Society of Biochemistry and Molecular Biology with International Participation / Strelec, Ivica ; Glavaš-Obrovac, Ljubica (ur.). - Osijek: Croatian Society of Biochemistry and Molecular Biology, 2008. 137.
/ - , 2008
Skup
CONGRESS OF THE CROATIAN SOCIETY OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
Mjesto i datum
Osijek, Hrvatska, 17.09.2008. - 20.09.2008
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
Arabidopsis; imunofilin; fotosinteza; PSII; fosforilacija; fotosintetski prijelaz stanja
(Arabidopsis; immunophilin; photosynthesis; PSII; phosphorylation; state-transitions)
Sažetak
Photosynthesis represents the crucial biochemical process responsible for the production of oxygen and food, and is carried out in two phases: a light and a dark phase. Chloroplasts, organelles in plant cells are responsible for photosynthesis. Chloroplast protein TLP40 (thylakoid lumen PPIase of 40 kDa), cychlophilin-like PPIase located in thylakoid lumen, was found to be involved in protein folding, biogenesis, and intraorganelle signaling. TLP40 shows peptidyl-prolyl cis-trans isomerase protein folding activity characteristic of immunophilins and was co-isolated with thylakoid membrane phosphatase from spinach. Gene coding CYP38 protein, ortholog of TLP40 from spinach, is located on the 3rd chromosome of Arabidopsis thaliana. To characterize the function of this protein in vivo, we analyzed knock-out Arabidopsis thaliana lines: cyp38-N and cyp38-M, which were screened for T-DNA insertion. Gene was interrupted by T-DNA insertion at position 1962 (6th exon) in cyp38-M, as confirmed by PCR and tested by Western blotting. Chlorophyll fluorescence measured in vivo with MINI-PAM portable chlorophyll fluorometer (Waltz) indicated slightly elevated non-photochemical quenching (NPQ) and considerably lowered relative electron transport rate (ETR) of mutants compared to wild-type plants. Also, PSII efficiency measured (Fv/Fm ratio), under normal light conditions was decreased in mutants. Analysis of chloroplast ultrastructure between CYP38 deficient and wild-type plants was performed, but no marked differences were observed. A quantitative state-transition measurements of intact rosetta leaves revealed that CYP38 gene inactivation leads to impaired state II transition implicating possible defects of antenna dephosphorylation in mutants lacking CYP38 protein.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
098-0982913-2838 - Regulatorni mehanizmi fotosinteze i diferencijacija plastida (Fulgosi, Hrvoje, MZOS ) ( CroRIS)
073-0731674-1673 - Utjecaj oksidativnog stresa na organizaciju i funkciju biljnih stanica i tkiva (Lepeduš, Hrvoje, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Hrvoje Lepeduš
(autor)
Hrvoje Fulgosi
(autor)
Ana Tomašić Paić
(autor)
Tatjana Prebeg
(autor)
Snježana Jurić
(autor)