http://www.cnr.it/ontology/cnr/individuo/prodotto/ID271973

Very rapid phosphorylation kinetics suggest a unique role for Lhcb2 during state transitions in Arabidopsis (Articolo in rivista)

Type

Label

Very rapid phosphorylation kinetics suggest a unique role for Lhcb2 during state transitions in Arabidopsis (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Claudia Leoni1-2, Malgorzata Pietrzykowska1, Anett Z. Kiss1, Marjaana Suorsa3, Luigi R. Ceci4, Eva-Mari Aro3 and Stefan Jansson1 (2013)
Very rapid phosphorylation kinetics suggest a unique role for Lhcb2 during state transitions in Arabidopsis
in Plant journal (Online); John Wiley & Sons, Ltd., Chichester (Regno Unito), Chichester (Regno Unito)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Claudia Leoni1-2, Malgorzata Pietrzykowska1, Anett Z. Kiss1, Marjaana Suorsa3, Luigi R. Ceci4, Eva-Mari Aro3 and Stefan Jansson1 (literal)

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1) Umea Plant Science Centre, Department of Plant Physiology, Umea University, 901 87 Umea, Sweden; 2) Department of Biosciences Biotechnologies and Pharmacology Sciences, Bari University, Via Amendola 165/A, 70126 Bari, Italy; 3) Department of Biochemistry and Food Chemistry, Molecular Plant Biology, University of Turku, FI-20014 Turku, Finland; 4) Institute of Biomembranes and Bioenergetics, CNR, Via Amendola 165/A, 70126 Bari, Italy (literal)

Titolo

Very rapid phosphorylation kinetics suggest a unique role for Lhcb2 during state transitions in Arabidopsis (literal)

Abstract

Light-harvesting complex II (LHCII) contains three highly homologous chlorophyll-a/b-binding proteins (Lhcb1, Lhcb2 and Lhcb3), which can be assembled into both homo- and heterotrimers. Lhcb1 and Lhcb2 are reversibly phosphorylated by the action of STN7 kinase and PPH1/TAP38 phosphatase in the so-called state-transition process. We have developed antibodies that are specific for the phosphorylated forms of Lhcb1 and Lhcb2. We found that Lhcb2 is more rapidly phosphorylated than Lhcb1: 10 sec of 'state 2 light' results in Lhcb2 phosphorylation to 30% of the maximum level. Phosphorylated and non-phosphorylated forms of the proteins showed no difference in electrophoretic mobility and dephosphorylation kinetics did not differ between the two proteins. In state 2, most of the phosphorylated forms of Lhcb1 and Lhcb2 were present in super- and mega-complexes that comprised both photosystem (PS)I and PSII, and the state 2-specific PSI-LHCII complex was highly enriched in the phosphorylated forms of Lhcb2. Our results imply distinct and specific roles for Lhcb1 and Lhcb2 in the regulation of photosynthetic light harvesting. (literal)

Editore