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  • 1.
    Edvardsson, Anna
    et al.
    Linköpings universitet.
    Petersson, Ulrika A.
    Södertörn University, School of Life Sciences. Stockholms universitet.
    Shapiguzov, Alexey
    Linköpings universitet.
    Schröder, Wolfgang P
    Södertörn University, School of Life Sciences. Umeå universitet.
    Vener, Alexander V.
    Linköpings universitet.
    Knockout of the cyclophilin AtCYP20-2 is compensated by oxidative activation of PPIase activity in the thylakoid lumen of Arabidopsis thalianaManuscript (preprint) (Other academic)
  • 2. Funk, C
    et al.
    Wiklund, R
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap.
    Jansson, C
    D1' centers are less efficient than normal photosystem II centers2001In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 505, no 1, p. 113-117Article in journal (Refereed)
    Abstract [en]

    One prominent difference between the photosystem II (PSII) reaction center protein D1 ' in Synechocystis 6803 and normal D1 is the replacement of Phe-186 in D1 with leucine in D1 '. Mutants of Synechocystis 6803 producing only D1 ', or containing engineered D1 proteins with Phe-186 substitutions, were analyzed by 77 K fluorescence emission spectra, chlorophyll a fluorescence induction yield and decay kinetics, and flash-induced oxygen evolution. Compared to D1-containing PSII centers, D1 ' centers exhibited a 50% reduction in variable chlorophyll a fluorescence yield, while the flash-induced O-2 evolution pattern was unaffected. In the F186 mutants, both the P680(+)/Q(A)(-) recombination and O-2 oscillation pattern were noticeably perturbed.

  • 3.
    Goulas, Estelle
    et al.
    Umeå universitet / Université des Sciences et Technologies de Lille 1, France.
    Schubert, Maria
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Kieselbach, Thomas
    Umeå universitet.
    Kleczkowski, Leszek A.
    Umeå universitet.
    Gardeström, Per
    Umeå universitet.
    Schröder, Wolfgang P
    Umeå universitet.
    Hurry, Vaughan
    Umeå universitet.
    The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature2006In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 47, no 5, p. 720-734Article in journal (Refereed)
    Abstract [en]

    Cold acclimation and over-wintering by herbaceous plants are energetically expensive and are dependent on functional plastid metabolism. To understand how the stroma and the lumen proteomes adapt to low temperatures, we have taken a proteomic approach (difference gel electrophoresis) to identify proteins that changed in abundance in Arabidopsis chloroplasts during cold shock (1 day), and short- (10 days) and long-term (40 days) acclimation to 5 degrees C. We show that cold shock (1 day) results in minimal change in the plastid proteomes, while short-term (10 days) acclimation results in major changes in the stromal but few changes in the lumen proteome. Long-term acclimation (40 days) results in modulation of the proteomes of both compartments, with new proteins appearing in the lumen and further modulations in protein abundance occurring in the stroma. We identify 43 differentially displayed proteins that participate in photosynthesis, other plastid metabolic functions, hormone biosynthesis and stress sensing and signal transduction. These findings not only provide new insights into the cold response and acclimation of Arabidopsis, but also demonstrate the importance of studying changes in protein abundance within the relevant cellular compartment.

  • 4.
    Kieselbach, T
    et al.
    Karolinska Institutet.
    Bystedt, Maria
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Hynds, P
    University of Warwick, UK.
    Robinson, C
    University of Warwick, UK.
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap.
    A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen2000In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 480, no 2-3, p. 271-276Article in journal (Refereed)
    Abstract [en]

    A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies shamed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively, In addition, novel isoforms of PsbO and PsbQ were identified.

  • 5.
    Petersson, Ulrika
    et al.
    Södertörn University, School of Life Sciences. Stockholms universitet.
    Horn, Ruth
    Umeå universitet.
    Schröder, Wolfgang P
    Södertörn University, School of Life Sciences. Umeå universitet.
    Comparative proteomics of oxidative stressed Arabidopsis thaliana thylakoid membranesManuscript (preprint) (Other academic)
  • 6.
    Schubert, Maria
    et al.
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institute.
    Petersson, Ulrika A
    Södertörn University, Avdelning Naturvetenskap. Stockholm University.
    Haas, B J
    Institute for Genomic Research, Rockville, USA.
    Funk, C
    Stockholm University.
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap.
    Kieselbach, T
    Karolinska Institute.
    Proteome map of the chloroplast lumen of Arabidopsis thaliana2002In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, no 10, p. 8354-8365Article in journal (Refereed)
    Abstract [en]

    The thylakoid membrane of the chloroplast is the center of oxygenic photosynthesis. To better understand the function of the luminal compartment within the thylakoid network, we have carried out a systematic characterization of the luminal thylakoid proteins from the model organism Arabidopsis thaliana. Our data show that the thylakoid lumen has its own specific proteome, of which 36 proteins were identified. Besides a large group of peptidyl-prolyl cis-trans isomerases and pro. teases, a family of novel PsbP domain proteins was found. An analysis of the luminal signal peptides showed that 19 of 36 luminal precursors were marked by a twin-arginine motif for import via the Tat pathway. To compare the model organism Arabidopsis with another typical higher plant, we investigated the proteome from the thylakoid lumen of spinach and found that the luminal proteins from both plants corresponded well. As a complement to our experimental investigation, we made a theoretical prediction of the luminal proteins from the whole Arabidopsis genome and estimated that the thylakoid lumen of the chloroplast contains similar to80 proteins.

  • 7.
    Schubert, Maria
    et al.
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Schröder, Wolfgang P.
    Umeå universitet.
    The TL29 protein a proposed ascorbate regulator in the thylakoid lumen of Arabidopsis thalianaManuscript (preprint) (Other academic)
  • 8. Shi, L X
    et al.
    Kim, S J
    Marchant, A
    Robinson, C
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institute.
    Characterisation of the PsbX protein from Photosystem II and light regulation of its gene expression in higher plants1999In: Plant Molecular Biology, ISSN 0167-4412, E-ISSN 1573-5028, Vol. 40, no 4, p. 737-744Article in journal (Refereed)
    Abstract [en]

    The location and expression of the previously uncharacterised photosystem II subunit PsbX have been analysed in higher plants. We show that this protein is a component of photosystem II (PSII) core particles but absent from light-harvesting complexes or PSII reaction centres. PsbX is, however, localised to the near vicinity of the reaction centre because it can be cross-linked to cytochrome b559, which is known to be associated with the D1/D2 dimer. We also show that the expression of this protein is tightly regulated by light, since neither protein nor mRNA is found in dark-grown plants.

  • 9. Shi, L X
    et al.
    Lorkovic, Z J
    Oelmuller, R
    Schröder, Wolfgang P
    The low molecular mass PsbW protein is involved in the stabilization of the dimeric photosystem II complex in Arabidopsis thaliana2000In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 275, no 48, p. 37945-37950Article in journal (Refereed)
    Abstract [en]

    Arabidopsis thaliana plants have been transformed with an antisense gene to the psbW of photosystem II (PSII). Eight transgenic lines containing low levels of psbW mRNA have been obtained. Transgenic seedlings with low contents of PsbW protein (more than 96% reduced) were selected by Western blotting and used for photosynthetic functional studies. There were no distinct differences in phenotype between the antisense and wild type plants during vegetative period under normal growth light intensities. However, a sucrose gradient separation of briefly solubilized thylakoid membranes revealed that no dimeric PSII supracomplex could be detected in the transgenic plants lacking the PsbW protein. Furthermore, analysis of isolated thylakoids demonstrated that the oxygen-evolving rate in antisense plants decreased by 50% compared with the wild type, This was found to be due to up to 40% of D1 and D2 reaction center proteins of PSII disappearing in the transgenic plants. The absence of the PsbW protein also altered the contents of other PSII proteins to differing extents. These results show that in the absence of the PsbW protein, the stability of the dimeric PSII is diminished and consequently the total number of PSII complexes is greatly reduced. Thus the nuclear encoded PsbW protein may play a crucial role in the biogenesis and regulation of the photosynthetic apparatus.

  • 10.
    Thidholm, Ellinor
    et al.
    Södertörn University, Avdelning Naturvetenskap.
    Lindström, V
    Tissier, C
    Robinson, C
    Schröder, Wolfgang P
    Södertörn University, Avdelning Naturvetenskap.
    Funk, C
    Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer2002In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 513, no 2-3, p. 217-222Article in journal (Refereed)
    Abstract [en]

    A blue-native gel electrophoresis system was combined with an in organello import assay to specifically analyse the location and assembly of two nuclear-encoded photosystem 11 (PSII) subunits. With this method we were able to show that initially the low molecular mass PsbW protein is not associated with the monomeric form of PSII. Instead a proportion of newly imported PsbW is directly assembled in dimeric PSH super-complexes with very fast kinetics; its negatively charged N-terminal domain is essential for this process. The chlorophyll-binding PsbS protein, which is involved in energy dissipation, is first detected in the monomeric PSII subcomplexes, and only at later time points in the dimeric form of PSII. It seems to be bound tighter to the PSII core complex than to light harvesting complex II. These data point to radically different assembly pathways for different PSII subunits.

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