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Mucin‐type O‐glycosylation – putting the pieces together
Author(s) -
Jensen Pia H.,
Kolarich Daniel,
Packer Nicolle H.
Publication year - 2010
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07429.x
Subject(s) - glycosylation , mucin , glycan , biochemistry , chemistry , n linked glycosylation , consensus sequence , amino acid , peptide sequence , sequence (biology) , glycoprotein , computational biology , biology , gene
The O‐glycosylation of Ser and Thr by N ‐acetylgalactosamine‐linked (mucin‐type) oligosaccharides is often overlooked in protein analysis. Three characteristics make O‐linked glycosylation more difficult to analyse than N‐linked glycosylation, namely: (a) no amino acid consensus sequence is known; (b) there is no universal enzyme for the release of O‐glycans from the protein backbone; and (c) the density and number of occupied sites may be very high. For significant biological conclusions to be drawn, the complete picture of O‐linked glycosylation on a protein needs to be determined. This review specifically addresses the analytical approaches that have been used, and the challenges remaining, in the characterization of both the composition and structure of mucin‐type O‐glycans, and the determination of the occupancy and heterogeneity at each amino acid attachment site.