Glycoprotein fucosyl transferase in the endoplasmic reticulum of castor bean endosperm cells

Roberts, Lynne M.; Mellor, Robert B.; Lord, J. Michael

doi:10.1016/0014-5793(80)80502-3

Cited by 10 publications

(5 citation statements)

References 19 publications

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“…That the linkage for the xylan synthesized by membranes from hypocotyls is mainly [1 -4] has been confirmed by periodate oxidation (Table 1), which produced an increasing proportion of radioactive glycerol to xylose with increasing time of oxidation, reaching 82% in glycerol after 12 days. Other products were apparently formed in addition to polysaccharide during the incubations (Table 2); incorporation into these fractions was much less than that found in some other glycosylating plant systems (Green & Northcote, 1979a;Mellor & Lord, 1979;Roberts et al, 1980;Barr & Nordin, 1980;Lehle, 1981). Conventional fractionation by t.l.c., ion-exchange chromatography on DEAE-cellulose and investigations by hydrolysis with phosphatase/phosphodiesterase (Bolwell & Northcote, 1981) did not indicate any significant incorporation into material that behaved as a polyprenyl phosphate monosaccharide or oligosaccharide in the material formed either with UDPxylose or with UDP-arabinose.…”

Section: Characterization Of Products Of Incorporation Of Udp-sugars mentioning

confidence: 89%

Arabinan synthase and xylan synthase activities of Phaseolus vulgaris. Subcellular localization and possible mechanism of action

Bolwell¹,

Northcote²

1983

Biochemical Journal

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Membrane fractions from bean hypocotyl or suspension cultures incorporated arabinose from UDP-beta-L-arabinose into arabinan and xylose from UDP-alpha-D-xylose in vitro; the level of each activity was dependent on the state of differentiation of the cells. These activities may be due to single transglycosylases, since no lipid or proteinaceous intermediate acceptors were found in either case. Subcellular fractionation studies showed that enzyme activity in vitro was localized in both Golgi-derived membranes and endoplasmic reticulum in similar amounts. However, incorporation into the polymers in vivo in suspension culture cells incubated with [1-3H]arabinose was considerably greater in the Golgi-derived membranes. Thus, although these enzymes may be translated and inserted at the level of the endoplasmic reticulum, their activities are under other levels of control, so that most of the activity in vivo is confined to the Golgi apparatus. Initiation of glycosylation in the endoplasmic activity may, however, occur.

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Section: Characterization Of Products Of Incorporation Of Udp-sugars mentioning

confidence: 89%

Arabinan synthase and xylan synthase activities of Phaseolus vulgaris. Subcellular localization and possible mechanism of action

Bolwell¹,

Northcote²

1983

Biochemical Journal

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“…The hydrophilic protein solution was mixed with an equivalent volume of cold 20%1o (w/w) TCA. After standing on ice for 30 min, the precipitated proteins were collected by centrifugation and retained for electrophoretic analysis.…”

Section: Methodsmentioning

confidence: 99%

Heterogeneous Distribution of Glycosyltransferases in the Endoplasmic Reticulum of Castor Bean Endosperm

Conder¹,

Lord²

1983

Plant Physiol.

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Endoplasmic reticulum membranes stripped of attached ribosomes were isolated from homogenates of germinating castor bean (Ricinus commuwus L.) endosperm by sucrose density gradient centrifuation. The isolated endoplasmic reticulum fraction was further separated into two major membrane subfractions by centfifugation on a flotation gradient. Both subfractions appeared to be derived from the endoplasmic reticulum inasmuch as they share several enzymk markers including cholinephosphotransferase, NADH-cytochrome c reductase, and glycoprotein fucosyltransferase and phase separation of membrane pobpptides using Triton X-114 revealed a stiking similarity in both their hydrophilk and hydrophobic protein components. The endoplasmic reticulum membrane subfractions contain glycoproteins which were readily labeled by incubating intact endosperm tissue with radioactive sugars prior to fractionation.Castor bean eadosperm endoplasmic reticulum apparently exhibits a degree of enzymk heterogeneity, however, since the enzymes responsible for the synthesis of dolicholpyrophosphate N-acetylglucosamine and dolicholmonophosphate mannose together with their incorporation into the oligosaccharde-Jipid precursor of protein N-glycosylation were largely recovered in a single endoplasmic reticulum subfraction.

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“…Unfortunately, the unusual phylogenetic relationship exhibited by known and putative plant FUTs will complicate the functional characterization of additional FUTs in diverse plant species. Tables FUT Type Plant Species Citation α-(1,3) FUT Zea mays Bondili et al, 2006 α-(1,4) FUT Silene alba Léonard et al, 2005 α-(1,4) FUT Vaccinium myrtillus L. Palma et al, 2001 α-(1,4) FUT Mangifera indica L. Okada et al, 2017 Undetermined Ricinus communis Roberts, Mellor and Lord, 1980 A multiple sequence alignment of the amino acid sequences of these genes was truncated from position 1-340 and from positions 1,156-1,178 to omit large, poorly resolved gaps in the alignment. The truncated alignment was then used to make a phylogenetic tree by Neighbor-Joining with 200 bootstraps and rooted with a Physcomitrella clade consisting of the genes Physcomitrella|Pp3c6_13740V3.1 and Physcomitrella|Pp3c6_13730V3.1; both the alignment and tree were made in Geneious.…”

Section: Plant Fut Phylogenymentioning

confidence: 99%

Plant Fucosyltransferases and the Emerging Biological Importance of Fucosylated Plant Structures

Soto

Urbanowicz

Hahn

2019

Critical Reviews in Plant Sciences

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Plants frequently incorporate the monosaccharide L-fucose (Fuc; 6-deoxy-Lgalactose) into glycans and glycopolymers located in diverse cellular locations. The incorporation of Fuc onto these varied glycans is carried out by fucosyltransferases (FUTs), that make up a protein superfamily with equally varied and diverse functions. The structures wherein Fuc is found have numerous proposed and validated functions, ranging from plant growth and development, cell expansion, adhesion and signaling, to energy metabolism, among others. FUTs from several different plant species have been identified and described; however, very few of them have been extensively characterized biochemically and biologically. In this review, we summarize plant FUTs that have been biochemically characterized and biologically investigated for associated phenotypes, offering greater insight and understanding into the physiological importance of Fuc in plants and in plant cell wall structures, glycans, and proteins.

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Glycoprotein fucosyl transferase in the endoplasmic reticulum of castor bean endosperm cells

Cited by 10 publications

References 19 publications

Arabinan synthase and xylan synthase activities of Phaseolus vulgaris. Subcellular localization and possible mechanism of action

Arabinan synthase and xylan synthase activities of Phaseolus vulgaris. Subcellular localization and possible mechanism of action

Heterogeneous Distribution of Glycosyltransferases in the Endoplasmic Reticulum of Castor Bean Endosperm

Plant Fucosyltransferases and the Emerging Biological Importance of Fucosylated Plant Structures

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