Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms

Kelleher, Daniel J.; Banerjee, Sulagna; Cura, Anthony J.; Samuelson, John; Gilmore, Reid

doi:10.1083/jcb.200611079

Cited by 45 publications

(45 citation statements)

References 39 publications

(86 reference statements)

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“…[13][14][15][16][17] Higher eukaryotes have evolved multiprotein complex OTases, in which subunits are involved in selection of mature glycan substrate and regulation of activity. [18][19][20] Duplication and divergence of multiprotein OTase subunits has also occurred, with genes encoding Stt3p and Ost3/6p proteins present in two copies in some organisms. 4 Two isoforms of OTase are present in yeast, defined by the presence of either of the homologous proteins Ost3p or Ost6p, 21 that differ in their protein substrate-specific activities at the level of individual glycosylation sites.…”

Section: Introductionmentioning

confidence: 99%

Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p

et al. 2011

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Asparagine-linked glycosylation is a common and vital co-and post-translocational modification of diverse secretory and membrane proteins in eukaryotes that is catalyzed by the multiprotein complex oligosaccharyltransferase (OTase). Two isoforms of OTase are present in Saccharomyces cerevisiae, defined by the presence of either of the homologous proteins Ost3p or Ost6p, which possess different protein substrate specificities at the level of individual glycosylation sites. Here we present in vitro characterization of the polypeptide binding activity of these two subunits of the yeast enzyme, and show that the peptide-binding grooves in these proteins can transiently bind stretches of polypeptide with amino acid characteristics complementary to the characteristics of the grooves. We show that Ost6p, which has a peptide-binding groove with a strongly hydrophobic base lined by neutral and basic residues, binds peptides enriched in hydrophobic and acidic amino acids. Further, by introducing basic residues in place of the wild type neutral residues lining the peptide-binding groove of Ost3p, we engineer binding of a hydrophobic and acidic peptide. Our data supports a model of Ost3/6p function in which they transiently bind stretches of nascent polypeptide substrate to inhibit protein folding, thereby increasing glycosylation efficiency at nearby asparagine residues.

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Section: Introductionmentioning

confidence: 99%

Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p

et al. 2011

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“…It can be chemically cross-linked to peptides derivatized with photoactivatable groups (Yan and Lennarz 2002;Nilsson et al 2003), and its bacterial and protist homologs transfer glycans to protein substrates (Wacker et al 2002;Kelleher and Gilmore 2006;Kelleher et al 2007;Nasab et al 2008;Hese et al 2009). Ost3 and Ost6 have a lumenal thioreductase fold with a CXXC motif common to proteins involved in disulfide bond shuffling during oxidative protein folding , and the proteins likely form transient disulfide bonds with nascent proteins and promote efficient glycosylation of Asn-X-Ser/Thr sites by delaying oxidative protein folding (Schulz and Aebi 2009;.…”

Section: N-glycosylationmentioning

confidence: 99%

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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The wall gives a Saccharomyces cerevisiae cell its osmotic integrity; defines cell shape during budding growth, mating, sporulation, and pseudohypha formation; and presents adhesive glycoproteins to other yeast cells. The wall consists of b1,3-and b1,6-glucans, a small amount of chitin, and many different proteins that may bear N-and O-linked glycans and a glycolipid anchor. These components become cross-linked in various ways to form higher-order complexes. Wall composition and degree of cross-linking vary during growth and development and change in response to cell wall stress. This article reviews wall biogenesis in vegetative cells, covering the structure of wall components and how they are cross-linked; the biosynthesis of N-and O-linked glycans, glycosylphosphatidylinositol membrane anchors, b1,3-and b1,6-linked glucans, and chitin; the reactions that cross-link wall components; and the possible functions of enzymatic and nonenzymatic cell wall proteins. TABLE OF CONTENTS Abstract 775Introduction 777

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“…Kinetic models that are based on in vitro studies predict that substrate selection for fully glucosylated LLOs is accomplished by the OST complex via an allosteric regulation involving a regulatory and a catalytic binding site for the LLO substrate (Pathak et al 1995;Karaoglu et al 2001;Kelleher et al 2007). Studies performed with mammalian OSTs led to insights into possible functions of other complex subunits.…”

Section: Functions Of Ost Subunitsmentioning

confidence: 99%

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

Breitling

Aebi

2013

Cold Spring Harbor Perspectives in Biology

226

191

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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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Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms

Cited by 45 publications

References 39 publications

Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p

Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

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