http://www.cnr.it/ontology/cnr/individuo/prodotto/ID296046
Surface-exposed Glycoproteins of Hyperthermophilic Sulfolobus solfataricus P2 Show a Common N-Glycosylation Profile (Articolo in rivista)
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- Surface-exposed Glycoproteins of Hyperthermophilic Sulfolobus solfataricus P2 Show a Common N-Glycosylation Profile (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/pr400123z (literal)
- Alternative label
Palmieri, Gianna; Balestrieri, Marco; Peter-Katalinic, Jasna; Pohlentz, Gottfried; Rossi, Mose; Fiume, Immacolata; Pocsfalvi, Gabriella (2013)
Surface-exposed Glycoproteins of Hyperthermophilic Sulfolobus solfataricus P2 Show a Common N-Glycosylation Profile
in Journal of proteome research (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Palmieri, Gianna; Balestrieri, Marco; Peter-Katalinic, Jasna; Pohlentz, Gottfried; Rossi, Mose; Fiume, Immacolata; Pocsfalvi, Gabriella (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Natl Res Council Italy; University of Munster; University of Rijeka; University of Munster (literal)
- Titolo
- Surface-exposed Glycoproteins of Hyperthermophilic Sulfolobus solfataricus P2 Show a Common N-Glycosylation Profile (literal)
- Abstract
- Cell surface proteins of hyperthermophilic Archaea actively participate in intercellular communication, cellular uptake, and energy conversion to sustain survival strategies in extreme habitats. Surface (S)-layer glycoproteins, the major component of the S-layers in many archaeal species and the best-characterized prokaryotic glycoproteins, were shown to have a large structural diversity in their glycan compositions. In spite of this, knowledge on glycosylation of proteins other than S-layer proteins in Archaea is quite limited. Here, the N-glycosylation pattern of cell-surface-exposed proteins of Sulfolobus solfataricus P2 were analyzed by lectin affinity purification, HPAEC-PAD, and multiple mass spectrometry-based techniques. Detailed analysis of SSO1273, one of the most abundant ABC transporters present in the cell surface fraction of S. solfataricus, revealed a novel glycan structure composed of a branched sulfated heptasaccharide, Hex(4)(GlcNAc)(2) plus sulfoquinovose where Hex is D-mannose and D-glucose. Having one monosaccharide unit more than the glycan of the S-layer glycoprotein of S. acidocaldarius, this is the most complex archaeal glycan structure known today. SSO1273 protein is heavily glycosylated and all 20 theoretical N-X-S/T (where X is any amino acid except proline) consensus sequence sites were confirmed. Remarkably, we show that several other proteins in the surface fraction of S. solfataricus are N-glycosylated by the same sulfated oligosaccharide and we identified 56 N-glycosylation sites in this subproteome. (literal)
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