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A previosly found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of photosystem I and is designated PSI-P
Plant Biochemistry Laboratory, Department of Plant Biology, The Royal Veterinary and Agricultural University, Copenhagen, Denmark.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
Department of Biology, Plant Physiology and Molecular Biology, University of Turku, Turku, Finland.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
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2005 (Engelska)Ingår i: FEBS Letters, ISSN 0014-5793, Vol. 579, nr 21, s. 4808-4812Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

We show that the thylakoid membrane phosphoprotein TMP14 is a novel subunit of plant photosystem I (PSI). Blue native/SDS–PAGE and sucrose gradient fractionation demonstrated the association of the protein exclusively with PSI. We designate the protein PSI-P. The presence of PSI-P subunit in Arabidopsis mutants lacking other PSI subunits was analyzed and suggested a location in the proximity of PSI-L, -H and -O subunits. The PSI-P protein was not differentially phosphorylated in state 1 and state 2.

Ort, förlag, år, upplaga, sidor
2005. Vol. 579, nr 21, s. 4808-4812
Nyckelord [en]
Photosystem I; Protein phosphorylation; State transitions; Thylakoids; Arabidopsis
Nationell ämneskategori
Medicin och hälsovetenskap
Identifikatorer
URN: urn:nbn:se:liu:diva-13860DOI: 10.1016/j.febslet.2005.07.061OAI: oai:DiVA.org:liu-13860DiVA, id: diva2:21931
Tillgänglig från: 2006-09-07 Skapad: 2006-09-07
Ingår i avhandling
1. Molecular characterization of protein phosphorylation in plant photosynthetic membranes
Öppna denna publikation i ny flik eller fönster >>Molecular characterization of protein phosphorylation in plant photosynthetic membranes
2006 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

Higher plants cannot move to a more favorable place when the environmental conditions are changing. To adapt to changes in light, temperature and access to water the plants had to evolve special mechanisms at the molecular level. Post-translational modifications of proteins, like phosphorylation, often serve as “on-and-off” switches in regulation of cellular activity and may affect protein-protein interactions. Photosynthesis in higher plants is regulated by reversible protein phosphorylation events, in a unique light- and redox-controlled system. Several biochemical methods are effectively used for characterization of phosphorylated proteins in photosynthetic membranes. Nevertheless, mass spectrometry is the most effective technique when it comes to identification of exact phosphorylation site(s) in the protein sequence, which is the ultimate evidence of protein phosphorylation. The same tandem mass spectrometry analysis identifies other in vivo post-translational modifications as well, such as acetylation of the N-terminus of mature protein. To study membrane proteins is a challenging project. In the present work the “shaving” of surface-exposed part of the membrane proteins, where phosphorylation occur, is used. In combination with mass spectrometry, this technique does not require the use of radioactive labeling or antibodies. The present work in spinach and Arabidopsis thaliana has identified and characterized several known phosphoproteins, new phosphorylation sites in well-known photosynthetic proteins, as well as two phosphoproteins previously unknown to be present in the photosynthetic membrane. Several photosystem II (PSII) core proteins become phosphorylated in their N-termini (D1, D2, CP43, PsbH), process involved in the regulation of the repair cycle of photo-damaged PSII complexes. The protein-protein interactions between PSII and its light harvesting complex (LHCII) seem to be affected by phosphorylation events in the interface area. In higher plants, phosphorylation sites have been identified in LHCII polypeptides, in one of the proteins (CP29) present in the interface area, as well as in the peripheral TSP9 protein. The TSP9 protein is unique among photosynthetic phosphoproteins, since it is a plant-specific soluble protein that becomes triple-phosphorylated in the middle part of the protein. It is also shown that photosystem I (PSI) is subjected to protein phosphorylation. The extrinsic PSI subunit PsaD becomes phosphorylated in its N-terminus. In addition, the latest characterized subunit of PSI, PsaP, is identified as a phosphoprotein. PsaP is an intrinsic protein assembled on the same side of the PSI complex as LHCII attaches. Several kinases are involved in phosphorylation of photosynthetic proteins, some more specific to PSII core proteins whereas others recognize LHCII proteins better. The STN8 kinase does not phosphorylate LHCII proteins, but is involved in the phosphorylation of the PSII core proteins D1, D2, CP43 and PsbH. STN8 is light-activated and is also specific in phosphorylation of threonine-4 (Thr-4) in the PsbH protein, but only after another kinase has phosphorylated Thr-2 first. A common feature of all kinases in plant photosynthetic membranes is the specificity for Thr residues and that the phosphorylation reactions occur in the N-terminal sequence of the proteins, except for the TSP9 protein. Nowadays, research is on the way to solve the complex network of regulation of photosynthetic activity via protein phosphorylation, but far more efforts are needed to get a complete view of the importance of all phosphorylation events and enzymatic specificity.

Serie
Linköping University Medical Dissertations, ISSN 0345-0082 ; 959
Nyckelord
protein phosphorylation, photosynthesis, mass spectrometry, protein characterization
Nationell ämneskategori
Cell- och molekylärbiologi
Identifikatorer
urn:nbn:se:liu:diva-6665 (URN)91-85497-92-4 (ISBN)
Disputation
2006-10-13, Linden, HU, ing 65, Hälsouniversitetet, Linköping, 09:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2006-09-07 Skapad: 2006-09-07 Senast uppdaterad: 2018-01-13

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Hansson, MariaVainonen, Julia P.Vener, Alexander V.

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