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  • 1.
    Eriksson, Charlotta
    et al.
    Södertörn University, School of Chemistry, Biology, Geography and Environmental Science. Karolinska Institute.
    Rustum, Cecilia
    Södertörn University, School of Chemistry, Biology, Geography and Environmental Science. Stockholm University.
    Hallberg, Einar
    Södertörn University, School of Chemistry, Biology, Geography and Environmental Science.
    Dynamic properties of nuclear pore complex proteins in gp210 deficient cells2004In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 572, no 1-3, p. 261-265Article in journal (Refereed)
    Abstract [en]

    Gp210, an integral membrane protein of the nuclear pore complex (NPC), is believed to be involved in NPC biogenesis. To test this hypothesis, we have investigated dynamic properties of the NPC and distribution of NPC proteins in NIH/ 3T3 cells lacking gp210. POM121 (the other integral NPC protein) and NUP107 (of the NUP107/160 complex) were correctly distributed at the nuclear pores in the absence of gp210. Furthermore, fluorescence recovery after photobleaching experiments showed that POM121 and NUP107 remained stably associated at the NPCs. We conclude that gp210 cannot be required for incorporation of POM121 or NUP107 or be required for maintaining NPC stability.

  • 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. Glaser, Elzbieta
    et al.
    Eriksson, AnnaCarin
    Sjöling, Sara
    Bifunctional role of the bc1 complex in plants Mitochondrial bc1 complex catalyses both electron transport and protein processing1994In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 346, no 1, p. 83-87Article in journal (Refereed)
    Abstract [en]

    Abstract Nuclear  encoded  mitochondrial  precursor  proteins  are  cleaved  to  mature  size products  by the  general  mitochondrial  processing  peptidase  (MPP). In  contrast  to  non-plant  sources  where  MPP  is  a matrix  enzyme,  the  plant  mitochondrial  MPP  is localised  in  the  inner  membrane  and  constitutes an  integral  part  of  the  bc,  complex  of  the  respiratory  chain.  Core  proteins  of  the  complex  are  immunologically  related  and  show  high  sequence similarity  to the MPP  subunits  from  non-plant  sources.  The bc,  complex  in plants  is thus  bifunctional,  being  involved  both  in respiration  and  in protein processing

  • 4. Grimm, T
    et al.
    Teglund, Stephan
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Tackels, D
    Sangiorgi, E
    Gurrieri, F
    Schwartz, C
    Toftgard, R
    Genomic organization and embryonic expression of Suppressor of Fused, a candidate gene for the split-hand/split-foot malformation type 32001In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 505, no 1, p. 13-17Article in journal (Refereed)
    Abstract [en]

    The genes for human and mouse Suppressor of Fused (SU(FU)/Su(Fu)) in the Hedgehog signaling pathway were characterized and found to contain 12 exons. Human SU(FU) localized on chromosome 10q24-25 between the markers D10S192 and AFM183XB12. We detected three additional SU(FU) isoforms, two of which have lost their ability to interact with the transcription factor GLI1. Expression analysis using whole mount in situ hybridization revealed strong expression of Su(Fu) in various mouse embryonic tissues. SU(FU) was considered a candidate gene for the split-hand/split-foot malformation type 3 (SHFM3). However, no alterations in the SU(FU) gene were found in SHFM3 patients.

  • 5. Jimenez, A
    et al.
    Johansson, C
    Ljung, J
    Sagemark, Johan
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Berndt, Kurt D
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Ren, B
    Tibbelin, G
    Ladenstein, R
    Kieselbach, T
    Holmgren, A
    Gustafsson, J A
    Miranda-Vizuete, A
    Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity2002In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 530, no 1-3, p. 79-84Article in journal (Refereed)
    Abstract [en]

    Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found exclusively in the tail of elongating spermatids and spermatozoa. We describe here further biochemical characterization of human Sptrx-1 protein structure and enzymatic activity. In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure. Analysis of circular dichroism spectra of fragments 1-360 and 361-469 and comparison to spectra of full-length Sptrx-1 supports a two-domain organization with a largely unstructured N-terminal domain and a folded thioredoxin-like C-terminal domain. Functionally, Sptrx-1 behaves as an oxidant in vitro when using selenite, but not oxidized glutathione, as electron acceptor. This oxidizing enzymatic activity suggests that Sptrx-1 might govern the stabilization (by disulfide cross-linking) of the different structures in the developing tail of spermatids and spermatozoa.

  • 6.
    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.

  • 7.
    Miranda-Vizuete, Antonio
    et al.
    Södertörn University, School of Life Sciences.
    Fierro Gonzalez, Juan Carlos
    Södertörn University, School of Life Sciences.
    Gahmon, Gabriele
    Burghoorn, Jan
    Södertörn University, School of Life Sciences.
    Navas, Plácido
    Swoboda, Peter
    Södertörn University, School of Life Sciences.
    Lifespan decrease in a Caenorhabditis elegans mutant lacking TRX-1, a thioredoxin expressed in ASJ sensory neurons2006In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 2, p. 484-490Article in journal (Refereed)
    Abstract [en]

    Thioredoxins are a class of small proteins that play a key role in regulating many cellular redox processes. We report here the characterization of the first member of the thioredoxin family in metazoans that is mainly associated with neurons. The Caenorhabditis elegans gene B0228.5 encodes a thioredoxin (TRX-1) that is expressed in ASJ ciliated sensory neurons, and to some extent also in the posterior-most intestinal cells. TRX-1 is active at reducing protein disulfides in the presence of a heterologous thioredoxin reductase. A mutant worm strain carrying a null allele of the trx-1 gene displays a reproducible decrease in both mean and maximum lifespan when compared to wild-type. The identification and characterization of TRX-1 paves the way to use C elegans as an in vivo model to study the role of thioredoxins in lifespan and nervous system physiology and pathology.

  • 8. Nordstrand, K
    et al.
    Åslund, F
    Meunier, S
    Holmgren, A
    Otting, G
    Berndt, Kurt D
    Karolinska Institutet.
    Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond1999In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 449, no 2-3, p. 196-200Article in journal (Refereed)
    Abstract [en]

    The active site of Escherichia coli glutaredoxin-3 (Grx3) consists of two redox active cysteine residues in the sequence -C-11-P-Y-C-14-H-. The H-1 NMR resonance of the cysteine thiol proton of Cys-14 in reduced Grx3 is observed at 7.6 ppm. The large downfield shift and NOEs observed with this thiol proton resonance suggest the presence of a hydrogen bond with the Cvs-ll thiolate, which is shown to have an abnormally low pK(a) value. A hydrogen bond would also agree,vith activity data of Grx3 active site mutants. Furthermore, the activity is reduced in a Grx3 H15V mutant, indicating electrostatic contributions to the stabilization of the Cys-ll thiolate, (C) 1999 Federation of European Biochemical Societies.

  • 9.
    Petersson, Ulrika A.
    et al.
    Södertörn University, School of Life Sciences.
    Kieselbach, Thomas
    Garcia-Cerdan, Jose G.
    Schroder, Wolfgang P.
    The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome2006In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 26, p. 6055-6061Article in journal (Refereed)
    Abstract [en]

    Peroxiredoxins; have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.

  • 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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