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Submitted on August 28, 2001
Branch of the Novartis Research Foundation, Friedrich Miescher Institute for Biomedical Research, Basel CH-4058
Corresponding Author: hofsteenge{at}fmi.ch
The final chemical structure of a newly synthesized protein is often only attained after further covalent modification. Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications, and often by the lack of suitable analysis methods. Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation. Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the axonal guidance protein rF-spondin. Nano-ESI-MSMS of isolated peptides showed that 8 out of 10 Trp residues in the TSRs of F-spondin are C-mannosylated. O-fucosylation sites were determined by a recently established nano-ESI Q-TOF MSMS approach. Four out of 5 TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites. In analogy to thrombospondin-1, we assume this to be Glc-Fuc-O-Ser/Thr. Our current knowledge of these glycosylations will be discussed.
Revised on September 17, 2001
Accepted on September 19, 2001
C-mannosylation and O-fucosylation of thrombospondin type 1 repeats
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