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  • 1.
    Baumann, Martin J.
    et al.
    KTH, School of Biotechnology (BIO).
    Eklöf, Jens M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Michel, Gurvan
    Kallas, Åsa M.
    KTH, School of Biotechnology (BIO).
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Czjzek, Mirjam
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: Biological implications for cell wall metabolism2007In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 19, no 6, p. 1947-1963Article in journal (Refereed)
    Abstract [en]

    High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen ( Populus tremula 3 Populus tremuloides). Production of the loop deletion variant Tm-NXG1-Delta YNIIG yielded an enzyme that was structurally similar to Ptt- XET16-34 and had a greatly increased transglycosylation: hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.

  • 2. Bourquin, V.
    et al.
    Nishikubo, N.
    Abe, H.
    Brumer, Harry
    KTH, Superseded Departments, Biotechnology.
    Denman, S.
    Eklund, M.
    Christiernin, M.
    Teeri, Tuula T.
    KTH, Superseded Departments, Biotechnology.
    Sundberg, B.
    Mellerowicz, E. J.
    Xyloglucan endotransglycosylases have a function during the formation of secondary cell walls of vascular tissues2002In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 14, no 12, p. 3073-3088Article in journal (Refereed)
    Abstract [en]

    Xyloglucan transglycosylases (XETs) have been implicated in many aspects of cell wall biosynthesis, but their function in vascular tissues, in general, and in the formation of secondary walls, in particular, is less well understood. Using an in situ XET activity assay in poplar stems, we have demonstrated XET activity in xylem and phloem fibers at the stage of secondary wall formation. Immunolocalization of fucosylated xylogucan with CCRC-M1 antibodies showed that levels of this species increased at the border between the primary and secondary wall layers at the time of secondary wall deposition. Furthermore, one of the most abundant XET isoforms in secondary vascular tissues (PttXET16A) was cloned and immunolocalized to fibers at the stage of secondary wall formation. Together, these data strongly suggest that XET has a previously unreported role in restructuring primary walls at the time when secondary wall layers are deposited, probably creating and reinforcing the connections between the primary and secondary wall layers. We also observed that xylogucan is incorporated at a high level in the inner layer of nacreous walls of mature sieve tube elements.

  • 3. Eklund, D. Magnus
    et al.
    Staldal, Veronika
    Valsecchi, Isabel
    Cierlik, Izabela
    Eriksson, Caitriona
    Hiratsu, Keiichiro
    Ohme-Takagi, Masaru
    Sundstrom, Jens F.
    Thelander, Mattias
    Ezcurra, Ines
    KTH, School of Biotechnology (BIO), Glycoscience.
    Sundberg, Eva
    The Arabidopsis thaliana STYLISH1 Protein Acts as a Transcriptional Activator Regulating Auxin Biosynthesis2010In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 22, no 2, p. 349-363Article in journal (Refereed)
    Abstract [en]

    The establishment and maintenance of auxin maxima in vascular plants is regulated by auxin biosynthesis and polar intercellular auxin flow. The disruption of normal auxin biosynthesis in mouse-ear cress ( Arabidopsis thaliana) leads to severe abnormalities, suggesting that spatiotemporal regulation of auxin biosynthesis is fundamental for normal growth and development. We have shown previously that the induction of the SHORT-INTERNODES/STYLISH (SHI/STY) family member STY1 results in increased transcript levels of the YUCCA (YUC) family member YUC4 and also higher auxin levels and auxin biosynthesis rates in Arabidopsis seedlings. We have also shown previously that SHI/STY family members redundantly affect development of flowers and leaves. Here, we further examine the function of STY1 by analyzing its DNA and protein binding properties. Our results suggest that STY1, and most likely other SHI/STY members, are DNA binding transcriptional activators that target genes encoding proteins mediating auxin biosynthesis. This suggests that the SHI/STY family members are essential regulators of auxin-mediated leaf and flower development. Furthermore, the lack of a shoot apical meristem in seedlings carrying a fusion construct between STY1 and a repressor domain, SRDX, suggests that STY1, and other SHI/STY members, has a role in the formation and/or maintenance of the shoot apical meristem, possibly by regulating auxin levels in the embryo.

  • 4. Gerttula, S.
    et al.
    Zinkgraf, M.
    Muday, G. K.
    Lewis, D. R.
    Ibatullin, Farid M.
    KTH, School of Biotechnology (BIO), Glycoscience. National Research Center Kurchatov Institute, Russian Federation.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience. University of British Columbia, Canada.
    Hart, F.
    Mansfield, S. D.
    Filkov, V.
    Groover, A.
    Transcriptional and hormonal regulation of gravitropism of woody stems in populus2015In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 27, no 10, p. 2800-2813Article in journal (Refereed)
    Abstract [en]

    Angiosperm trees reorient their woody stems by asymmetrically producing a specialized xylem tissue, tension wood, which exerts a strong contractile force resulting in negative gravitropism of the stem. Here, we show, in Populus trees, that initial gravity perception and response occurs in specialized cells through sedimentation of starch-filled amyloplasts and relocalization of the auxin transport protein, PIN3. Gibberellic acid treatment stimulates the rate of tension wood formation and gravibending and enhances tissue-specific expression of an auxin-responsive reporter. Gravibending, maturation of contractile fibers, and gibberellic acid (GA) stimulation of tension wood formation are all sensitive to transcript levels of the Class I KNOX homeodomain transcription factor-encoding gene ARBORKNOX2 (ARK2). We generated genome-wide transcriptomes for trees in which gene expression was perturbed by gravistimulation, GA treatment, and modulation of ARK2 expression. These data were employed in computational analyses to model the transcriptional networks underlying wood formation, including identification and dissection of gene coexpression modules associated with wood phenotypes, GA response, and ARK2 binding to genes within modules. We propose a model for gravitropism in the woody stem in which the peripheral location of PIN3-expressing cells relative to the cambium results in auxin transport toward the cambium in the top of the stem, triggering tension wood formation, while transport away from the cambium in the bottom of the stem triggers opposite wood formation.

  • 5.
    Grenville-Briggs, Laura J.
    et al.
    Aberdeen Oomycete Group, University of Aberdeen, Institute of Medical Sciences.
    Anderson, Victoria L.
    Aberdeen Oomycete Group, University of Aberdeen, Institute of Medical Sciences.
    Fugelstad, Johanna
    KTH, School of Biotechnology (BIO), Glycoscience.
    Avrova, Anna O.
    Plant-Pathology Programme, Scottish Crop Research Institute, Invergowrie, Dundee.
    Bouzenzana, Jamel
    Organisation et Dynamique des Membranes Biologiques, Unité Mixte de Recherche 5246, Université Lyon I.
    Williams, Alison
    Aberdeen Oomycete Group, University of Aberdeen, Institute of Medical Sciences.
    Wawra, Stephan
    Aberdeen Oomycete Group, University of Aberdeen, Institute of Medical Sciences.
    Whisson, Stephen C.
    Plant-Pathology Programme, Scottish Crop Research Institute, Invergowrie, Dundee.
    Birch, Paul R. J.
    Plant-Pathology Programme, Scottish Crop Research Institute, Invergowrie, Dundee.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    van West, Pieter
    Aberdeen Oomycete Group, University of Aberdeen, Institute of Medical Sciences.
    Cellulose synthesis in Phytophthora infestans is required for normal appressorium formation and successful infection of potato2008In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 20, no 3, p. 720-738Article in journal (Refereed)
    Abstract [en]

    Cellulose, the important structural compound of cell walls, provides strength and rigidity to cells of numerous organisms. Here, we functionally characterize four cellulose synthase genes (CesA) in the oomycete plant pathogen Phytophthora infestans, the causal agent of potato (Solanum tuberosum) late blight. Three members of this new protein family contain Pleckstrin homology domains and form a distinct phylogenetic group most closely related to the cellulose synthases of cyanobacteria. Expression of all four genes is coordinately upregulated during pre- and early infection stages of potato. Inhibition of cellulose synthesis by 2,6-dichlorobenzonitrile leads to a dramatic reduction in the number of normal germ tubes with appressoria, severe disruption of the cell wall in the preinfection structures, and a complete loss of pathogenicity. Silencing of the entire gene family in P. infestans with RNA interference leads to a similar disruption of the cell wall surrounding appressoria and an inability to form typical functional appressoria. In addition, the cellulose content of the cell walls of the silenced lines is >50% lower than in the walls of the nonsilenced lines. Our data demonstrate that the isolated genes are involved in cellulose biosynthesis and that cellulose synthesis is essential for infection by P. infestans.

  • 6. Johansson, P.
    et al.
    Brumer, Harry
    KTH, Superseded Departments, Biotechnology.
    Baumann, Martin J.
    KTH, Superseded Departments, Biotechnology.
    Kallas, Åsa
    KTH, Superseded Departments, Biotechnology.
    Henriksson, Hongbin
    KTH, Superseded Departments, Biotechnology.
    Denman, Stuart
    KTH, Superseded Departments, Biotechnology.
    Teeri, Tuula
    KTH, Superseded Departments, Biotechnology.
    Jones, A.
    Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of the transglycosylation acceptor binding2004In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 16, no 4, p. 874-886Article in journal (Refereed)
    Abstract [en]

    Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-Angstrom resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transgilycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.

  • 7. Niculaes, Claudiu
    et al.
    Morreel, Kris
    Kim, Hoon
    Lu, Fachuang
    Mckee, Lauren S.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ivens, Bart
    Haustraete, Jurgen
    Vanholme, Bartel
    De Rycke, Riet
    Hertzberg, Magnus
    Fromm, Jörg
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Polle, Andrea
    Ralph, John
    Boerjan, Wout
    Phenylcoumaran Benzylic Ether Reductase Prevents Accumulation of Compounds Formed under Oxidative Conditions in Poplar Xylem2014In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 26, no 9, p. 3775-3791Article in journal (Refereed)
    Abstract [en]

    Phenylcoumaran benzylic ether reductase (PCBER) is one of the most abundant proteins in poplar (Populus spp) xylem, but its biological role has remained obscure. In this work, metabolite profiling of transgenic poplar trees downregulated in PCBER revealed both the in vivo substrate and product of PCBER. Based on mass spectrometry and NMR data, the substrate was identified as a hexosylated 8-5-coupling product between sinapyl alcohol and guaiacylglycerol, and the product was identified as its benzyl-reduced form. This activity was confirmed in vitro using a purified recombinant PCBER expressed in Escherichia coli. Assays performed on 20 synthetic substrate analogs revealed the enzyme specificity. In addition, the xylem of PCBER-downregulated trees accumulated over 2000-fold higher levels of cysteine adducts of monolignol dimers. These compounds could be generated in vitro by simple oxidative coupling assays involving monolignols and cysteine. Altogether, our data suggest that the function of PCBER is to reduce phenylpropanoid dimers in planta to form antioxidants that protect the plant against oxidative damage. In addition to describing the catalytic activity of one of the most abundant enzymes in wood, we provide experimental evidence for the antioxidant role of a phenylpropanoid coupling product in planta.

  • 8. Onnerud, H.
    et al.
    Zhang, Liming
    KTH, Superseded Departments, Pulp and Paper Technology.
    Gellerstedt, Göran
    KTH, Superseded Departments, Pulp and Paper Technology.
    Henriksson, Gunnar
    KTH, Superseded Departments, Pulp and Paper Technology.
    Polymerization of monolignols by redox shuttle-mediated enzymatic oxidation: A new model in lignin biosynthesis I2002In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 14, no 8, p. 1953-1962Article in journal (Refereed)
    Abstract [en]

    Lignin is one of the most abundant biopolymers, and it has a complex racemic structure. It may be formed by a radical polymerization initiated by redox enzymes, but much remains unknown about the process, such as how molecules as large as enzymes can generate the compact structure of the lignified plant cell wall. We have synthesized lignin oligomers according to a new concept, in which peroxidase is never in direct contact with the lignin monomers coniferaldehyde and coniferyl alcohol. Instead, manganese oxalate worked as a diffusible redox shuttle, first being oxidized from Mn(II) to Mn(III) by a peroxidase and then being reduced to Mn(II) by a simultaneous oxidation of the lignin monomers to radicals that formed covalent linkages of the lignin type. Furthermore, a high molecular mass polymer was generated by oxidation of coniferyl alcohol by Mn(III) acetate in a dioxane and water mixture. This polymer was very similar to natural spruce wood lignin, according to its NMR spectrum. The possible involvement of a redox shuttle/peroxidase system in lignin biosynthesis is discussed.

  • 9. Pacheco-Villalobos, David
    et al.
    Diaz-Moreno, Sara M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    van der Schuren, Alja
    Tamaki, Takayuki
    Kang, Yeon Hee
    Gujas, Bojan
    Novak, Ondrej
    Jaspert, Nina
    Li, Zhenni
    Wolf, Sebastian
    Oecking, Claudia
    Ljung, Karin
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Hardtke, Christian S.
    The Effects of High Steady State Auxin Levels on Root Cell Elongation in Brachypodium2016In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 28, no 5, p. 1009-1024Article in journal (Refereed)
    Abstract [en]

    The long-standing Acid Growth Theory of plant cell elongation posits that auxin promotes cell elongation by stimulating cell wall acidification and thus expansin action. To date, the paucity of pertinent genetic materials has precluded thorough analysis of the importance of this concept in roots. The recent isolation of mutants of the model grass species Brachypodium distachyon with dramatically enhanced root cell elongation due to increased cellular auxin levels has allowed us to address this question. We found that the primary transcriptomic effect associated with elevated steady state auxin concentration in elongating root cells is upregulation of cell wall remodeling factors, notably expansins, while plant hormone signaling pathways maintain remarkable homeostasis. These changes are specifically accompanied by reduced cell wall arabinogalactan complexity but not by increased proton excretion. On the contrary, we observed a tendency for decreased rather than increased proton extrusion from root elongation zones with higher cellular auxin levels. Moreover, similar to Brachypodium, root cell elongation is, in general, robustly buffered against external pH fluctuation in Arabidopsis thaliana. However, forced acidification through artificial proton pump activation inhibits root cell elongation. Thus, the interplay between auxin, proton pump activation, and expansin action may be more flexible in roots than in shoots.

  • 10. Peltier, Jean-Benoît
    et al.
    Emanuelsson, Olof
    Stockholms universitet.
    Kalume, Dário E.
    Ytterberg, Jimmy
    Friso, Giulia
    Rudella, Andrea
    Liberles, David A.
    Söderberg, Linda
    Roepstorff, Peter
    von Heijne, Gunnar
    van Wijk, Klaas J
    Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction2002In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 14, no 1, p. 211-236Article in journal (Refereed)
    Abstract [en]

    Experimental proteome analysis was combined with a genome-wide prediction screen to characterize the protein content of the thylakoid lumen of Arabidopsis chloroplasts. Soluble thylakoid proteins were separated by two-dimensional electrophoresis and identified by mass spectrometry. The identities of 81 proteins were established, and N termini were sequenced to validate localization prediction. Gene annotation of the identified proteins was corrected by experimental data, and an interesting case of alternative splicing was discovered. Expression of a surprising number of paralogs was detected. Expression of five isomerases of different classes suggests strong (un)folding activity in the thylakoid lumen. These isomerases possibly are connected to a network of peripheral and lumenal proteins involved in antioxidative response, including peroxiredoxins, m-type thioredoxins, and a lumenal ascorbate peroxidase. Characteristics of the experimentally identified lumenal proteins and their orthologs were used for a genome-wide prediction of the lumenal proteome. Lumenal proteins with a typical twin-arginine translocation motif were predicted with good accuracy and sensitivity and included additional isomerases and proteases. Thus, prime functions of the lumenal proteome include assistance in the folding and proteolysis of thylakoid proteins as well as protection against oxidative stress. Many of the predicted lumenal proteins must be present at concentrations at least 10,000-fold lower than proteins of the photosynthetic apparatus.

  • 11. Roberts, Alison W.
    et al.
    Lahnstein, Jelle
    Hsieh, Yves S. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Xing, Xiaohui
    Yap, Kuok
    Chaves, Arielle M
    Scavuzzo-Duggan, Tess R
    Dimitroff, George
    Lonsdale, Andrew
    Roberts, Eric M.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Fincher, Geoffrey B
    Doblin, Monika Susanne
    Bacic, Antony
    Burton, Rachel A
    Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan2018In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 30, no 6, p. 1293-1308Article in journal (Refereed)
    Abstract [en]

    Mixed-linkage (1,3;1,4)-β-glucan (MLG), an abundant cell wall polysaccharide in the Poaceae, has been detected in ascomycetes, algae, and seedless vascular plants, but not in eudicots. Although MLG has not been reported in bryophytes, a predicted glycosyltransferase from the moss Physcomitrella patens (Pp3c12_24670) is similar to a bona fide ascomycete MLG synthase. We tested whether Pp3c12_24670 encodes an MLG synthase by expressing it in wild tobacco (Nicotiana benthamiana) and testing for release of diagnostic oligosaccharides from the cell walls by either lichenase or (1,4)-β-glucan endohydrolase. Lichenase, an MLG-specific endohydrolase, showed no activity against cell walls from transformed N. benthamiana, but (1,4)-β-glucan endohydrolase released oligosaccharides that were distinct from oligosaccharides released from MLG by this enzyme. Further analysis revealed that these oligosaccharides were derived from a novel unbranched, unsubstituted arabinoglucan (AGlc) polysaccharide. We identified sequences similar to the P. patens AGlc synthase from algae, bryophytes, lycophytes, and monilophytes, raising the possibility that other early divergent plants synthesize AGlc. Similarity of P. patens AGlc synthase to MLG synthases from ascomycetes, but not those from Poaceae, suggests that AGlc and MLG have a common evolutionary history that includes loss in seed plants, followed by a more recent independent origin of MLG within the monocots.

  • 12. Schrader, J.
    et al.
    Nilsson, J.
    Mellerowicz, E.
    Berglund, A.
    Nilsson, Peter
    KTH, Superseded Departments, Biotechnology.
    Hertzberg, M.
    Sandberg, G.
    A high-resolution transcript profile across the wood-forming meristem of poplar identifies potential regulators of cambial stem cell identity2004In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 16, no 9, p. 2278-2292Article in journal (Refereed)
    Abstract [en]

    Plant growth is the result of cell proliferation in meristems, which requires a careful balance between the formation of new tissue and the maintenance of a set of undifferentiated stem cells. Recent studies have provided important information on several genetic networks responsible for stem cell maintenance and regulation of cell differentiation in the apical meristems of shoots and roots. Nothing, however, is known about the regulatory networks in secondary meristems like the vascular cambium of trees. We have made use of the large size and highly regular layered organization of the cambial meristem to create a high-resolution transcriptional map covering 220 mum of the cambial region of aspen (Populus tremula). Clusters of differentially expressed genes revealed substantial differences in the transcriptomes of the six anatomically homogenous cell layers in the meristem zone. Based on transcriptional and anatomical data, we present a model for the position of the stem cells and the proliferating mother cells in the cambial zone. We also provide sets of marker genes for different stages of xylem and phloem differentiation and identify potential regulators of cambial meristem activity. Interestingly, analysis of known regulators of apical meristem development indicates substantial similarity in regulatory networks between primary and secondary meristems.

  • 13. Tang, W. H.
    et al.
    Ezcurra, Inés
    KTH, Superseded Departments, Biotechnology.
    Muschietti, J.
    McCormick, S.
    A cysteine-rich extracellular protein, LAT52, interacts with the extracellular domain of the pollen receptor kinase LePRK22002In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 14, no 9, p. 2277-2287Article in journal (Refereed)
    Abstract [en]

    Pollen germination and pollen tube growth are thought to require extracellular cues, but how these cues are perceived and transduced remains largely unknown. Pollen receptor kinases are plausible candidates for this role; they might bind extracellular ligands and thereby mediate cytoplasmic events required for pollen germination and pollen tube growth. To search for pollen-expressed ligands for pollen receptor kinases, we used the extracellular domains of three pollen-specific receptor kinases of tomato (LePRK1, LePRK2, and LePRK3) as baits in a yeast two-hybrid screen. We identified numerous secreted or plasma membrane-bound candidate ligands. One of these, the Cys-rich protein LAT52, was known to be essential during pollen hydration and pollen tube growth. We used in vivo coimmunoprecipitation to demonstrate that LAT52 was capable of forming a complex with LePRK2 in pollen and to show that the extracellular domain of LePRK2 was sufficient for the interaction. Soluble LAT52 can exist in differently sized forms, but only the larger form can interact with LePRK2. We propose that LAT52 might be a ligand for LePRK2.

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