Elton John Best Concert Tickets at Covelli Centre in Youngstown, OH in Youngstown, Ohio For Sale

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Moss Mnium (Fry et al., xxxx), a few partial putative XTH sequences were revealed in the Physcomitrella patens genome (Rensing et al., xxxx; http://www.cosmoss.org) and expansin sequences were found in mosses as well (Schipper et al., xxxx; Yi et al., xxxx). To our knowledge, no data concerning the presence of XET activity in algae have been reported to date. To explore further the presence of XET activity, a broad range of bryophytes were examined and the potential origin of XET activity in green, red and brown algae was studied (Fig. The Bryophyta, Anthocerophyta and Marchantiophyta represent the oldest lineages among extant land plants and together they form the bryophytes (Fig. ). Given that the Physcomitrella genome is in the process of being sequenced, the XET search started with the Bryophyta, blasting the draft database (http://www.cosmoss.org) with Sk-XTH1 (Van Sandt et al., xxxx). This blast result included all hits that were also obtained when blasting with the different Arabidopsis XTHs. At least two of the resulting ESTs included all motifs that are essential for XET activity in vascular plants (Campbell and Braam, xxxx; Henriksson et al., xxxx; Johansson et al., xxxx, xxxx; Van Sandt et al., xxxx). A functional XET assay on Physcomitrella homogenate was performed to prove the presence of at least one functional XTH protein. XTH and its XET function are thus present in Physcomitrella patens and they are possibly encoded by a multi-gene family. An XTH-related cell-wall-modifying machinery is thus probably present throughout the mosses and perhaps even in evolutionary more primitive phyla.Specific XET activity was detected in other Bryophyta and in the Anthocerophyta and Marchantiophyta. Furthermore, in both the gametophyte and the sporophyte of the Bryophyta and Anthocerophyta and in the gametophyte of the Marchantiophyta, a clear correlation between the site of growth and the presence of XET activity was demonstrated. In the Bryophyta the pattern of XET activity in acrocarp mosses corresponds nicely with the developmental stage of the apical cell. A fluorescent XET signal is only present when a young gametophyte is pressed onto the test paper. In older acrocarps the apical cell is used to form a gametangium, causing the gametophyte to cease growth. In accordance, no XET activity was found at the site of the gametophyte apex in sporophyte-bearing gametophytes. Another illustration of the correlation between XET activity and growth was found in the sporophytes of the Anthocerophyta. These land plants have a near basal meristem (Renzaglia and Vaugh, xxxx; Shaw and Renzaglia, xxxx), and XET activity occurs specifically at the elongation site above the basal meristem of the sporophyte. In liverworts, considered to be the most ancient plant lineage (Kenrick and Crane, xxxx; Bateman et al., xxxx), a clear correlation between XET activity and the sites of growth was observed.Although significant differences exist in cell wall composition of the major land plant lineages, xyloglucan was found in the primary cell wall of all land plants, including the bryophytes (Popper and Fry, xxxx, xxxx). The conservation of the XET substrate throughout land plant evolution fits nicely with the conservation of XET function within land plants. It is therefore likely that XET activity is part of an ancient cell-wall-modifying machinery that originated even before the divergence of land plants.The descent of the embryophytes from a charophyte ancestor (Fig. ) is among others supported by the presence of cellulose-synthesizing rosettes in both groups (Hotchkiss and Brown, xxxx). Charophytic algae were shown to lack xyloglucan (Popper and Fry, xxxx). Remarkably, an unambiguous XET signal was present near to or below the meristematic cells of both apex and branchlets of the Chara vulgaris tissue print. Although xyloglucan was found to be absent in charophycean algae (Popper and Fry, xxxx), some Chara cell wall enzymes seem to be able to catalyse the incorporation of xyloglucan oligosaccharides into the xyloglucan matrix on the test paper, and thus display XET activity. Recent studies have demonstrated a structural connection between XTHs and xylan endohydrolases. Based upon these findings it was suggested that XTHs could be active not only on cell wall xyloglucan but also on xylans (Strohmeier et al., xxxx; Nishitani and Vissenberg, xxxx). Interestingly, the enzymatic digests of the Chara AIR (alcohol insoluble residue) resulted in products corresponding with the oligosaccharides of xylan (Popper and Fry, xxxx). The presence of genes coding for XTHs or XTH-like enzymes that in vivo transglucosylate xylans or other hemicelluloses in Chara was therefore studied. 3' RACE, using a degenerate primer based upon the variations present in angiosperm XTHs, resulted in the amplification of a 480-bp fragment, named Chara2. To study its homology with XTHs, Chara2 was aligned with angiosperm XTHs (monocots and dicots). As recent data suggest an evolutionary link between 1,3-1,4-ß-d-endoglucanases and XTHs (Strohmeier et al., xxxx), 1,3-1,4-ß-d-endoglucanases were included in the alignment as well. In addition to a homologous three-dimensional topology of the active site amino acids, as seen for XTHs and endoxylanases, 1,3-1,4-ß-d-endoglucanases share the same amino acid composition with XTHs. Both enzyme families are therefore thought to share a common ancestor (Strohmeier et al., xxxx). Aligning Chara2 with representatives of both enzyme families revealed that Chara2 shares features of both XTHs and 1,3-1,4-ß-d-endoglucanases. The key differences between XTHs and 1,3-1,4-ß-d-endoglucanases are the presence of a PYX motif in XTHs and the substitution of a methionine in 1,3-1,4-ß-d-endoglucanases by a tyrosine in XTHs (Strohmeier et al., xxxx). Chara2 has one of the two possible substitutions (M?Y), positioning it between both groups. The PYX motif, however, is not necessary for the XET function, as AtXTH4, an XTH that was shown to display XET activity, lacks this motif (Campbell and Braam, xxxx). An additional difference between XTHs and 1,3-1,4-ß-d-endoglucanases is a region in the protein that forms the acceptor binding loop in XTHs. In Chara2 this region is more similar to that of XTHs than in 1,3-1,4-ß-d-endoglucanases (Fig. , shaded). Again, this positions Chara2 between both groups of enzymes. Together these data suggest that Chara2 is possibly the C-terminal end of an enzyme that is an intermediate between 1,3-1,4-ß-d-endoglucanases, present in microbial organisms, and XTHs, seen in vascular plants. This is also reflected in the positioning of the Chara2 amino acid sequence within XTHs and 1,3-1,4-ß-d-endoglucanases in a phylogenetic tree (data not shown). The Chara XTH-like enzyme and its interacting donor substrate therefore probably evolved together to an optimal enzyme?substrate interacting model as is seen in higher plants. The evolution to a XyG/XTH interacting mechanism was possibly one of the crucial events allowing the development of land plants.Remarkably, a tissue print of Ulva linza, an ulvophycean alga belonging to the Chlorophyte lineage of the green plants, also showed a clear XET signal. The fluorescent spot corresponded to a small region above the holdfast of the algae. This holdfast is formed by the basal cell dividing into 3?4 holdfast cells, which elongate and undergo further division (Kim et al., xxxx). A clear correlation between cell elongation and transglucosylation activity is therefore even found in the Chlorophyte lineage of green plants. Analysis of the cell wall components from Ulva lactuca and Ulva rigida suggested the presence of cellulose microfibrils associated with XyG-like polysaccharides (Lahaye et al., xxxx). The structure of this sulfated glucuronorhamnoxyloglucan (ulvan) is, however, markedly different from that of higher plants (Lahaye and Ray, xxxx). In other studies a 1,3-1,4-ß-d-glucan endohydrolase digest of the Ulva AIR was shown to contain glucose and xylose (Popper and Fry, xxxx), indicating the presence of a mixed linkage glucan with xylose substitutions in the Ulva cell wall. In accordance with the findings in the Charophyta, an ancient chlorophyte XTH-like enzyme possibly interacts with the mixed linkage xyloglucan-like polysaccharide as donor substrate in Ulva linza. Again these findings are supported by the evolutionary connection between 1,3-1,4-ß-d-glucan endohydrolases and XTHs.It is possible that in the green algae transglucosylating enzymes with a broader substrate range were/are present that gave rise to the XTHs with a higher substrate specificity. Recently the reverse story was suggested in monocots, where XTHs are thought to have lost their substrate specificity and now transglucosylate 1,3-1,4-ß-d-glucans as well during growth and cell elongation (Strohmeier et al., xxxx). Similar to Chara2, these monocot XTHs (HvXTH4) miss some typical XTH features which possibly play a role in narrowing the substrate specificity (Fig. , arrows) and have a less conserved amino acid composition of their acceptor binding loop (Fig. , shaded). This could be proof of the close relationship and possible interconversions of XTHs and 1,3-1,4-ß-d-endoglucanases by small mutations. In addition, a mannan transglycosylase was detected in several plant species (Schroder et al., xxxx), but no sequences of responsible enzymes are yet known.In contrast to Ulva linza, no XET activity was found in Ulva lactuca. This difference in the presence of XET activity is striking. It can be explained by the fact that both organisms have a distinct morphology and growth pattern, being either tubular or planar. The Ulva lactuca specimen studied had a planar form where growth occurs in the entire plant body (http://www.algaebase.org). XET activity would therefore probably cause a very diffuse and hence undetectable XET signal, whereas growth and XET activity is more concentrated and detectable in the holdfast of the tubular growth form, as found in Ulva linza. The absence of a detectable XET signal in Cladophora rupestris, another Ulvophycean, supports this suggestion as the slender filaments could leave only a very faint and thus invisible XET signal on the test paper. This limitation of the technique to visualize XET activity in filamentous or unicellular organisms, as mentioned above, prevented further analysis of the presence of XET-related transglucosylation activity in the other major groups of chlorophytes and charophytes.The finding of XET-related activity in a chlorophytic species opens new ideas on the understanding of the evolution of green plants and gives new insights into the development of their cell wall. The XTH-modifying machinery therefore probably originated in the ancestors of both charophytes and chlorophytes, before the split of the green plants. The presence of XyG and preference of this hemicellulose as an XTH substrate, as seen in dicots, is probably the result of selecting an optimal enzyme?substrate interacting mechanism to allow efficient cell wall elongation. A future strategy allowing the study of XET-related activity in thread-like and unicellular organisms, such as Mesostigma (see Fig. ), could further clarify the phylogenetic relationship of the charophytes and chlorophytes and would reveal more details on the evolution of XET activity in green plants.The presence of XET activity in the major lineages of the green plants raised the question of the presence of XET-related growth mechanism in red and brown algae. No XET activity was detected on tissue prints of different red and brown algae. The colour of the autofluorescence caused by algae pigments differed enough from that of the SR substrates to allow the detection of possible XET activity. Furthermore, the absence of XET activity is in complete agreement with the composition of their primary cell walls. Although both phaeophytes and rhodophytes contain cellulose fibrils, no homologue of XyG, mixed linkage-ß-d-glucans and xylans can be found within their cell wall, suggesting another mechanism for cell wall expansion (Graham and Wilcox, xxxx).In summary, the data presented herein have revealed a clear correlation between growth (or cell elongation) and the presence of XET activity in all three major groups of bryophytes, and the presence of at least two potential XTH-encoding cDNAs in the Physcomitrella genome has been demonstrated. For the first time, it has been shown that XET activity is also present at sites of growth in Charophyta and Chlorophyta, suggesting that XET originated even before the evolutionary divergence of the Chlorobionta. In accordance, part of a transcript in Chara that possibly encodes an ancestral XTH enzyme was identified, and the structural and evolutionary link between XTHs, endo-xylanases and 1-3,1-4-ß-d-endoglucanases was discussed, explaining the substrate-tolerant behaviour of this ancient transglucosylating enzyme. As no XET activity was detected in the Phaeophyta and Rhodophyta, XET activity is probably a feature unique to green plants.V.V.S. is funded by a PhD grant of the Institute for the Promotion of Innovation through Science and Technology in Flanders (IWT ? Vlaanderen). K.V. is a Postdoctoral Fellow of the Fund for Scientific Research ? Flanders (FWO ? Vlaanderen). This research was partially funded by a University of Antwerp grant (UA-BOF) and a grant from the Fund for Scientific Research ? Flanders (FWO ? Vlaanderen), grant G.xxxx.04. We thank S. C. Fry for the labelled oligosaccharides, D. De Beer for his help in finding Phaeoceros carolinianus, Professor S. Hoste, Chairman of the Flemish Study group of Bryology and Lichenology, for his help in the collection of Anthoceros agrestis, Professor W. De Smet for the collection of marine algae and the Fund for Scientific Research ? Flanders (FWO ? Vlaanderen) for financial support.Albert M, Werner M, Proksch P, Fry SC, Kaldenhoff R. The cell wall-modifying xyloglucan endotransglycosylase/hydrolase LeXTH1 is expressed during the defence reaction of tomato against the plant parasite. Cuscuta reflexa. Plant Biology. xxxx;6:402?407. [PubMed]Bateman RM, Crane PR, Dimichelle WA, Kenrick PR, Rowe NP, Speck T, Stein WE. Early evolution of land plants: phylogeny, physiology, and ecology of the primary terrestrial radiation. Annual Review of Systematics. xxxx;29:263?292.Buck WR, Goffinet BG. Morphology and classification of mosses. In: Shaw AJ, Goffinet B, editors. Bryophyte biology. Cambridge: Cambridge University Press; xxxx. pp. 71?123.Campbell P, Braam J. Co- and/or post-translational modifications are critical for TCH4 XET activity. Plant Journal. xxxx;15:553?561. [PubMed]Campbell P, Braam J. Xyloglucan endotransglycosylases: diversity of genes, enzymes and potential wall-modifying functions. Trends in Plant Science. xxxx;4:361?366.Carpita NC, Gibeaut DM. Structural models of primary-cell walls in flowering plants consistency of molecular structures with the physical properties of the wall during growth. Plant Journal. xxxx;3:1?30. [PubMed]Crandall-Stotler B, Stotler RE. Morphology and classification of the Marchantiophyta. In: Shaw AJ, Goffinet B, editors. Bryophyte biology. Cambridge: Cambridge University Press; xxxx. pp. 21?70.Goffinet BG, Buck WR. Goffinet BG, Hollowell V, Magill R, editors. Systematics of Bryophyta (mosses): from molecules to revised classification. Molecular systematics of bryophytes. Monographs in Systematic Botany from the Missouri Botanical Garden. xxxx;98:205?239.Graham LE, Wilcox LW. Algae. New York: Prentice Hall; xxxx. Graham LE, Cook M, Busse J. The origin of plants: body plan changes contributing to a major evolutionary radiation. Proceedings of the National Academy of Sciences of the USA. xxxx;97:xxxx?xxxx. [PMC free article] [PubMed]Hayashi T, Marsden MPF, Delmer D. Pea xyloglucan and cellulose: VI. Xyloglucan-cellulose interactions in vitro and in vivo. Plant Physiology. xxxx;83:384?389. [PMC free article] [PubMed]Henriksson H, Denman SE, Campuzano DG, Ademark P, Master ER, Teeri TT, Brumer H. N-linked glycosylation of native and recombinant cauliflower xyloglucan endotransglycosylase 16A. Biochemical Journal. xxxx;375:61?73. [PMC free article] [PubMed]Henrissat B, Coutinho P, Davies G. A census of carbohydrate-active enzymes in the genome of. Arabidopsis thaliana. Plant Molecular Biology. xxxx;47:55?72. [PubMed]Hotchkiss AT, Jr, Brown RM., Jr The association of rosette and globule terminal complexes with cellulose microfibril assembly in Nitella translucens (Charophyceae) Journal of Phycology. xxxx;23:229?237.Hu Y, Poh HM, Chua NH. The Arabidopsis ARGOS-LIKE gene regulates cell expansion during organ growth. The Plant Journal. xxxx;47:1?9. [PubMed]Iannetta PPM, Fry SC. Visualization of the activity of xyloglucan endotransglycosylase (XET) isoenzymes after gel electrophoresis. Phytochemical Analysis. xxxx;10:238?240.Johansson P, Denman S, Brumer H, Kallas AM, Henriksson H, Bergfors T. Crystallization and preliminary X-ray analysis of a xyloglucan endotransglycosylase from Populus tremula×tremuloides. Acta Crystallographica. xxxx;59:535?537. [PubMed]Johansson P, Brumer H, Bauman MJ, Kallas AM, Henriksson H, Denman S. Crystal structures of a xyloglucan endotransglycosylase reveal details of transglycosylation acceptorbinding. Plant Cell. xxxx;16:874?886. [PMC free article] [PubMed]Kenrick PR, Crane PR. The origin and early evolution of plants on land. Nature. xxxx;389:33?39.Kim KY, Ahn YS, Lee IK. Growth and morphology of Enteromorpha linza (L.) J. Ag. and E. prolifera (Müller) J. Ag. (Ulvales, Chlorohyceae) Korean Journal of Phycology. xxxx;6:31?45.Lahaye M, Ray B. Cell-wall polysaccharides from the marine green alga Ulva ?rigida?
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Elton John
Caesars Palace - Colosseum
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Youngstown, OH
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