Structure, biosynthesis, and function of asparagine‐linked glycans on plant glycoproteins

Faye, Loı̈c; Johnson, Kenneth D.; Sturm, Arnd; Chrispeels, Maarten J.

doi:10.1111/j.1399-3054.1989.tb06187.x

Cited by 113 publications

(43 citation statements)

References 27 publications

(14 reference statements)

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“…These show that purification of proteins and cloning of cDNAs that originate through this route give rise to antibodies and cDNAs that can be used on the whole plant and locate to the predicted tissues and cells. Examples include structural proteins such as glycine-rich proteins (25), hydroxyproline-rich glycoproteins (5), proline-rich proteins (26), and enzymes such as peroxidases (23), chitinases, and laccases (27). Analyses of the sequences generated in this study validate the methodology, since many are known wall proteins and the cells remain intact.…”

Section: Discussionmentioning

confidence: 76%

Differential Extraction and Protein Sequencing Reveals Major Differences in Patterns of Primary Cell Wall Proteins from Plants

Robertson¹,

Mitchell²,

Gilroy³

et al. 1997

Journal of Biological Chemistry

123

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The proteins of the primary cell walls of suspension cultured cells of five plant species, Arabidopsis, carrot, French bean, tomato, and tobacco, have been compared. The approach that has been adopted is differential extraction followed by SDS-polyacrylamide gel electrophoresis (PAGE), rather than two-dimensional gel analysis, to facilitate protein sequencing. Whole cells were washed sequentially with the following aqueous solutions, CaCl 2 , CDTA (cyclohexane diaminotetraacetic acid, DTT (dithiothreitol), NaCl, and borate. SDS-PAGE analysis showed consistent differences between species. From the 233 proteins that were selected for sequencing, 63% gave N-terminal data. This analysis shows that (i) patterns of proteins revealed by SDS-PAGE are strikingly different for all five species, (ii) a large number of these proteins cannot be identified by data base searches indicating that a significant proportion of wall proteins have not been previously described, (iii) the major proteins that can be identified belong to very different classes of proteins, (iv) the majority of proteins found in the extracellular growth media are absent from their respective cell wall extracts, and (v) the results of the extraction process are indicative of higher order structure. It appears that aspects of speciation reside in the complement of extracellular wall proteins. The data represent a protein resource for cell wall studies complementary to EST (expressed sequence tag) and DNA sequencing strategies.The plant cell wall is a dynamic system generally considered to be composed of more than 90% carbohydrate polymers. Proteins, phenolics and possibly lipids make up the remainder of the wall (1-3). To date, most research interest has been in the carbohydrate components because of considerations of their structural role and commercial interest. This has led to a number of models for the integration, interpolymeric association, and assembly of the wall (3, 4). By comparison, our knowledge of the complexity of protein in the plant cell wall is in a less advanced state. Much of the understanding of the range of structural wall proteins has come from cDNA and genomic cloning exercises and has led to the identification of glycine-, cysteine-, proline-, and hydroxyproline-rich subsets of wall proteins. In addition, many extracellular enzymes have been identified that are required for the restructuring and modification of this dynamic extracellular matrix which underpin its role in defense, detoxification, signaling, cell-cell recognition, cell expansion, cell adhesion, cell separation, translocation, differentiation, and morphogenesis (2, 5, 6). However, there is a lack of direct studies on the proteins themselves and the true range of extracellular proteins and their species differences remains to be elucidated. The present work describes the systematic extraction and sequencing of the major primary wall proteins from five species representing four families of plants.Since whole plant tissue is complicated by the presence of different tissue...

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Section: Discussionmentioning

confidence: 76%

Differential Extraction and Protein Sequencing Reveals Major Differences in Patterns of Primary Cell Wall Proteins from Plants

Robertson¹,

Mitchell²,

Gilroy³

et al. 1997

Journal of Biological Chemistry

123

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“…Mature secretary proteins contain both high mannose glycans and complex glycans and the conversion of a high mannose glycan to a complex glycan occurs in the Golgi apparatus (9,15). The two types of glycans can be distinguished by their sensitivity to Endo H. Whether a high mannose glycan is converted to a complex glycan depends in part on its position and accessibility to the Golgi-modifying enzymes (10).…”

Section: Modification Of High Mannose Glycans To Complex Glycansmentioning

confidence: 99%

“…Glycans occur on many plant secretary proteins and the role that glycans play is still obscure (9). New evidence indicates that glycans help to stabilize protein conformation and protect proteins against breakdown (8).…”

Section: Role Of Glycosylationmentioning

confidence: 99%

The Signal Peptide of a Vacuolar Protein Is Necessary and Sufficient for the Efficient Secretion of a Cytosolic Protein

Hunt¹,

Chrispeels²

1991

Plant Physiol.

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A cytosolic pea (Pisum sativum) seed albumin (ALB) and a chimeric protein (PHALB) consisting of the signal peptide and first three amino acids of phytohemagglutinin (PHA) and the amino acid sequence of ALB were expressed in parallel suspension cultures of tobacco (Nicotiana tabacum) cells and their intracellular fates examined. PHALB was efficiently secreted by the cells whereas ALB remained intracellular. These experiments show that the information contained in the signal peptide of a vacuolar protein is both necessary and sufficient for efficient secretion, and define secretion as a default or bulk-flow pathway. Entry into the secretary pathway was accompanied by glycosylation and the efficient conversion of the high mannose glycans into complex glycans indicating that transported glycoproteins do not need specific recognition domains for the modifying enzymes in the Golgi. Tunicamycin depressed the accumulation of the unglycosylated polypeptide in the culture medium much less than the accumulation of other glycoproteins. We interpret this as evidence that glycans on proteins that are not normally glycosylated do not have the same function of stabilizing and protecting the polypeptide as on natural glycoproteins.The secretary system of plant cells delivers proteins to the vacuole, the tonoplast, the plasma membrane, and the cell wall/extracellular space. In addition, proteins that enter the secretary system may be retained in the endoplasmic reticulum or in various compartments of the Golgi complex. The first step common to the transport of all these proteins is translocation across the ER membrane (25). Once

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“…On the basis of substrate specificities of oligosaccharide-processing enzymes, recently Johnson and Chrispeels reported that fucosyl transferase may act in vitro as soon as the first GlcNAc residue is added to the Man5GlcNAc2 and xylosyl transferase acts after the removal of two mannosyl residues by a-mannosidase I1 in Phuseolus vulguris [20]. Furthermore, Faye et al presented the processing step in which fucosyl transferase acts on GlcNAcMan3GlcNAc2 and a xylose residue is added to GlcNAc2Man3GlcNAc (Fuc)GlcNAc by xylosyl transferase in plants [26]. Some processing enzymes in plant cells have been purified (glucosidase I [21], glucosidase I1 [22], amannosidase 1 [23], a-mannosidase I1 [24] and GlcNAc transferase I1 [25]), the biosynthetic pathway which is used to produce plant-specific oligosaccharides, however, has not yet to be completely clarified.…”

mentioning

confidence: 99%

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Tezuka

Hayashi

Ishihara

et al. 1992

European Journal of Biochemistry

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We measured the activities of a-I ,3-mannosyl-glycoprotein ~-l,2-N-acetylglucosaminyltransferase, a-1,6-mannosyl-glycoprotein p-1,2-N-acetylglucosaminyltransferase, ~-3,4-mannosyl-glycoprotein p-1,2-xylosyltransferase and glycoprotein 3-a-~-fucosyltransferase in the Golgi fraction of suspension-cultured cells of sycamore (Acer pseudoplatanus L.) using fluorescence-labelled oligosaccharides as acceptor substrates for these transferase reactions. The structures of the pyridylaminated oligosaccharides produced by these reactions were analyzed by two-dimensional sugar mapping using high-performance liquid chromatography. We demonstrated that The biosynthesis of oligosaccharides in animal cells has been well characterized [l]. This pathway starts from the transfer of Glc3Man9GlcNAc, to nascent polypeptide chains in the endoplasmic reticulum. The processing of Glc3Man9GlcNAcz begins with the removal of three glucose and four mannose residues by sequential reactions of a-glucosidases and aCorrespondence to N . Takahashi, Nagoya City University, College of Nursing, Mizuho-ku, Nagoya, Japan 467.Abbreviations. GlcNAc transferase I, a-I ,3-mannosyl-glycoprotcin ~-1,2-N-acetyIglucosaminyltransferase; GlcNAc transferase 11, a-1,6-mannosyl-glycoprotein ~-1,2-N-acetylglucosaminyltransferase; xylosyl transferase, ~-1,4-mannosyl-glycoprotein B-1,2-xylosyltransferase; fucosyl transferase, glycoprotein 3-a-~-fucosyltransferase; Fuc, fucose; UDP-Xyl, uridine(5')diphospho(l)-/?-xylose; GDP-Fuc, guanosine(5')diphospho-a-L-fucose.Enzymes. a-l,3-Mannosyl-glycoprotein ~-1,2-N-acetylglucosami- mannosidases. The product of these reactions, Man5-GlcNAc,, is the precursor of all N-acetyllactosamine-type oligosaccharides [2]. It is the substrate of GlcNAc transferase I which produces the first N-acetyllactosamine-type intermediate, GlcNAcMan,GlcNAcz. Various N-acetyllactosamine-type oligosaccharides found in animal glycoproteins are produced from GlcNAcMan5GlcNAcz after further modification by a-mannosidase 11, GlcNAc transferase, fucosyl transferase, galactosyl transferase and sialyl transferase. The structures of many oligosaccharides in plant glycoproteins have been elucidated during the last decade [3 -141. These works have revealed that xylose-containing oligosaccharides are widely distributed throughout the plant kingdom, although, xylose-containing N-linked oligosaccharides were also found in glycoproteins from gastropods [15, 161 and Chlorophyceae [17]. The biosynthesis of the oligosaccharide chains in plant glycoproteins has been recently investigatedThe biosynthesis of N-linked oligosaccharide in rice xamylase containing GlcNAc,Man3XylGlcNAcz has been par-

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Structure, biosynthesis, and function of asparagine‐linked glycans on plant glycoproteins

Cited by 113 publications

References 27 publications

Differential Extraction and Protein Sequencing Reveals Major Differences in Patterns of Primary Cell Wall Proteins from Plants

Differential Extraction and Protein Sequencing Reveals Major Differences in Patterns of Primary Cell Wall Proteins from Plants

The Signal Peptide of a Vacuolar Protein Is Necessary and Sufficient for the Efficient Secretion of a Cytosolic Protein

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

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