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The photosystem II light-harvesting protein Lhcb3 affects the macrostructure of photosystem II and the rate of state transitions in Arabidopsis
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik. Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå Plant Science Centre (UPSC).
Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands.
School of Biological and Chemical Sciences, Queen Mary University of London, London, E1 4NS, United Kingdom.
Institute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, H-6726 Szeged, Hungary.
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2009 (Engelska)Ingår i: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 21, s. 3245-3256Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The main trimeric light-harvesting complex of higher plants (LHCII) consists of three different Lhcb proteins (Lhcb1-3). We show that Arabidopsis thaliana T-DNA knockout plants lacking Lhcb3 (koLhcb3) compensate for the lack of Lhcb3 by producing increased amounts of Lhcb1 and Lhcb2. As in wild-type plants, LHCII-photosystem II (PSII) supercomplexes were present in Lhcb3 knockout plants (koLhcb3), and preservation of the LHCII trimers (M trimers) indicates that the Lhcb3 in M trimers has been replaced by Lhcb1 and/or Lhcb2. However, the rotational position of the M LHCII trimer was altered, suggesting that the Lhcb3 subunit affects the macrostructural arrangement of the LHCII antenna. The absence of Lhcb3 did not result in any significant alteration in PSII efficiency or qE type of nonphotochemical quenching, but the rate of transition from State 1 to State 2 was increased in koLhcb3, although the final extent of state transition was unchanged. The level of phosphorylation of LHCII was increased in the koLhcb3 plants compared with wild-type plants in both State 1 and State 2. The relative increase in phosphorylation upon transition from State 1 to State 2 was also significantly higher in koLhcb3. It is suggested that the main function of Lhcb3 is to modulate the rate of state transitions.

Ort, förlag, år, upplaga, sidor
2009. Vol. 21, s. 3245-3256
Identifikatorer
URN: urn:nbn:se:umu:diva-29921DOI: 10.1105/tpc.108.064006PubMedID: 19880802Scopus ID: 2-s2.0-72049130532OAI: oai:DiVA.org:umu-29921DiVA, id: diva2:278596
Tillgänglig från: 2009-11-27 Skapad: 2009-11-27 Senast uppdaterad: 2023-03-24Bibliografiskt granskad
Ingår i avhandling
1. Phosphorylation in State Transition: Less cause more effect
Öppna denna publikation i ny flik eller fönster >>Phosphorylation in State Transition: Less cause more effect
2011 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Alternativ titel[sv]
Fosforylering och "state transitions" : mindre orsak, mer verkan
Abstract [en]

Study of the Arabidopsis thaliana knockout mutant lacking Lhcb3 (koLhcb3) have revealed a close similarity to the wild type plants. Growth rate, NPQ, qP, Φ(PSII), circular dichroism spectra, pigment composition and content of LCHII trimers have been found to be unaffected by this mutation. The proteomic analysis shows only some minor increases in the amount of Lhcb1 and Lhcb2. PAM fluorometry revealed a significant increase in the rate of the state 1 to state 2 state transition in the koLhcb3. None the less, the extent of state transition is identical to wild type. Alterations in the PSII-LHCII supercomplex structure have been demonstrated as well. The M-trimer was found to be rotated ~21° CCW. This altered binding of the LHCII M-trimer is likely the cause of the altered affinity resulting in the increased rate of state transition. Proteomic analysis of the phosphorylation of LHCII revealed a significant increase in state 1 and 2 LHCII phosphorylation relative to wild type. Investigation whether phosphorylation or the altered LHCII binding is the cause of the accelerated rate of state transition have not been conclusive so far. A Lhcb6 depleted mutant (koLhcb6) showed a significant alteration of the PSII-LHCII supercomplex structure and photosynthetic acclimation processes. The LHCII M-trimer is depleted in the PSII-LHCII supercomplexes causing the state transition process to be “stuck” in state 2 and the mutants ability to preform NPQ is inhibited as well. The Lhcb6 protein was concluded to be essential for the binding of the LHCII M-trimer to the PSII core as well as energy transfer. The depletion of LHCII M-trimer was linked to the reduced ability to photoacclimate using NPQ as well.

Ort, förlag, år, upplaga, sidor
University of Umeå: Department of Plant Physiology, 2011. s. 56
Nyckelord
Photosynthesis, Photoacclimation, State Transtion, LHCII Phosphorylation, Lhcb3, Lhcb6
Nationell ämneskategori
Botanik
Forskningsämne
molekylärbiologi
Identifikatorer
urn:nbn:se:umu:diva-38870 (URN)978-91-7459-131-6 (ISBN)
Disputation
2011-01-28, Naturvetarhuset, N450, Umeå Universitet, Umeå, 10:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2011-01-05 Skapad: 2011-01-05 Senast uppdaterad: 2015-04-29Bibliografiskt granskad

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Damkjær, Jakob TKiss, Anett ZJansson, Stefan

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Institutionen för fysiologisk botanikUmeå Plant Science Centre (UPSC)
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The Plant Cell

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