N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells

Matsui, Toshimitsu; Takita, Eiji; Sato, Toshio; Kinjo, Satoko; Aizawa, Michie; Sugiura, Yukie; Hamabata, Takashi; Sawada, Kazutoshi; Kato, Ko

doi:10.1093/glycob/cwq198

Cited by 39 publications

(34 citation statements)

References 23 publications

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“…The acceptor peptide forms a 180°turn and the hydroxyl amino acid at the +2 position is recognized by a binding pocket of the enzyme formed by a highly conserved WWDYG motif found in the STT3 protein family [82]. Assuming that polypeptide substrate recognition of eukaryotic OST is similar to the bacterial enzyme (the conserved nature of the peptide binding site supports this hypothesis), the crystal structure of PglB explains the preferences of NxT over NxS for OST reactivity in vitro [83] as well as the use of rare non-canonical N-glycosylation sites found in N-glycoproteins [84][85][86][87][88][89][90].…”

Section: Substrate Specificity Of Oligosaccharyltransferasementioning

confidence: 92%

N-linked protein glycosylation in the ER

Aebi

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

609

516

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N-linked protein glycosylation in the endoplasmic reticulum (ER) is a conserved two phase process in eukaryotic cells. It involves the assembly of an oligosaccharide on a lipid carrier, dolichylpyrophosphate and the transfer of the oligosaccharide to selected asparagine residues of polypeptides that have entered the lumen of the ER. The assembly of the oligosaccharide (LLO) takes place at the ER membrane and requires the activity of several specific glycosyltransferases. The biosynthesis of the LLO initiates at the cytoplasmic side of the ER membrane and terminates in the lumen where oligosaccharyltransferase (OST) selects N-X-S/T sequons of polypeptide and generates the N-glycosidic linkage between the side chain amide of asparagine and the oligosaccharide. The N-glycosylation pathway in the ER modifies a multitude of proteins at one or more asparagine residues with a unique carbohydrate structure that is used as a signalling molecule in their folding pathway. In a later stage of glycoprotein processing, the same systemic modification is used in the Golgi compartment, but in this process, remodelling of the N-linked glycans in a protein-, cell-type and species specific manner generates the high structural diversity of N-linked glycans observed in eukaryotic organisms. This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

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Section: Substrate Specificity Of Oligosaccharyltransferasementioning

confidence: 92%

N-linked protein glycosylation in the ER

Aebi

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

609

516

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“…It can be assumed that similar structural constraints also hold true for eukaryotic OSTs, because proline also prohibits glycosylation of eukaryotic sequons. The conservation of the sequon is not absolute because glycosylation of nonconsensus sequons (NxC, NGx, and NxV) has been reported in nematodes, plants, and mammals, although these are rare (about 1% -2%) compared with NxT/ S sequons (Titani et al 1986;Miletich and Broze 1990;Vance et al 1997;Sato et al 2000;Kaji et al 2003;Zielinska et al 2010;Matsui et al 2011). NxT sequons are glycosylated more efficiently than NxS, whereas NxC sequons are only poorly modified by OST in vitro (Breuer et al 2001) and in vivo (Gavel and von Heijne 1990;Ben-Dor et al 2004;Zielinska et al 2010).…”

Section: Polypeptide Acceptor Substratesmentioning

confidence: 99%

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

Breitling

Aebi

2013

Cold Spring Harbor Perspectives in Biology

241

215

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The attachment of glycans to asparagine residues of proteins is an abundant and highly conserved essential modification in eukaryotes. The N-glycosylation process includes two principal phases: the assembly of a lipid-linked oligosaccharide (LLO) and the transfer of the oligosaccharide to selected asparagine residues of polypeptide chains. Biosynthesis of the LLO takes place at both sides of the endoplasmic reticulum (ER) membrane and it involves a series of specific glycosyltransferases that catalyze the assembly of the branched oligosaccharide in a highly defined way. Oligosaccharyltransferase (OST) selects the Asn-X-Ser/Thr consensus sequence on polypeptide chains and generates the N-glycosidic linkage between the side-chain amide of asparagine and the oligosaccharide. This ER-localized pathway results in a systemic modification of the proteome, the basis for the Golgi-catalyzed modification of the N-linked glycans, generating the large diversity of N-glycoproteome in eukaryotic cells. This article focuses on the processes in the ER. Based on the highly conserved nature of this pathway we concentrate on the mechanisms in the eukaryotic model organism Saccharomyces cerevisiae.

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“…thaliana T87 cultured cells were cultured in a modified Murashige-Skoog medium and genetically transformed using Agrobacterium tumefaciens EHA105, as described previously (Matsui et al 2011).…”

Section: Plant Material Transformation and Culture Conditionsmentioning

confidence: 99%

A Computational and Experimental Approach Reveals that the 5′-Proximal Region of the 5′-UTR has a Cis-Regulatory Signature Responsible for Heat Stress-Regulated mRNA Translation in Arabidopsis

Matsuura

Takenami

Kubo

et al. 2013

Plant and Cell Physiology

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Translation of specific plant mRNAs is differentially regulated under certain abiotic stress conditions such as heat, oxygen deprivation and dehydration. The majority of transcripts exhibit varying degrees of translational repression, whereas a subset of transcripts escape such repression and remain actively translated. The underlying mechanisms that mediate this control, and in particular the identities of the regulatory RNA elements involved, remain poorly understood. Using a combined computational and experimental approach, we identified a novel cis-regulatory element in the 5 0 -untranslated region (5 0 -UTR) that affects differential translation in response to heat stress (HS) in Arabidopsis thaliana. First, we selected a set of genes with distinct translational responses to HS, based on our previously reported genome-wide data regarding changes in polysome loading induced by HS in A. thaliana cultured cells. We evaluated the 5 0 -UTRs of these messages for their ability to mediate expression, when fused to reporter mRNAs, in protoplasts under HS. The data from the reporter assay and the nucleotide sequences of the 5 0 -UTRs tested were used to define regulatory elements in the 5 0 -UTRs, with the help of a partial least square (PLS) regression model. The computational analysis using PLS and subsequent experimental characterization of a series of 5 0 -UTR mutants provided evidence that the 5 0 -proximal sequence of the 5 0 -UTR is a primary and position-dependent determinant of 5 0 -UTR-mediated differential translation in response to HS. Finally, we discuss the possible mechanism underlying HS regulation of differential mRNA translation.

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N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells

Cited by 39 publications

References 23 publications

N-linked protein glycosylation in the ER

N-linked protein glycosylation in the ER

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

A Computational and Experimental Approach Reveals that the 5′-Proximal Region of the 5′-UTR has a Cis-Regulatory Signature Responsible for Heat Stress-Regulated mRNA Translation in Arabidopsis

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