R Shyama Prasad Rao, Ole Thomsen Buus, Bernd Wollenweber
Aarhus University, Department of Genetics and Biotechnology, Slagelse, Denmark. drrsprao@yahoo.co.in
Computational biology and chemistry 2011 AprN-glycosylation is a common protein modification process, which affects a number of properties of proteins. Little is known about the distribution of N-glycosylation sequons, for example, the distance between glycosylated sites and their position in the protein primary sequence. Using a large set of experimentally confirmed eukaryotic N-glycoproteins we analyzed the relative position and distribution of sequons. N-Glycosylation probability was found to be lower in the termini of protein sequences compared to the mid region. N-glycosylated sequons were found much farther from C terminus compared to the N-terminus of the protein sequence and this effect was more pronounced for NXS sequons. The distribution of sequons, modeled based on balls-in-boxes classical occupancy, showed a near-maximum probability. Considerable proportion of sequons was found within a distance of ten amino acids, indicating that the steric hindrance was not a key factor in protein N-glycosylation. Interestingly, the distribution of all sequons present in N-glycoproteins showed a pattern very similar to that of glycosylated sequons. The results indicate that protein N-glycosylation chiefly follows a random design. Copyright © 2011 Elsevier Ltd. All rights reserved.
R Shyama Prasad Rao, Ole Thomsen Buus, Bernd Wollenweber. Distribution of N-glycosylation sequons in proteins: how apart are they? Computational biology and chemistry. 2011 Apr;35(2):57-61
PMID: 21353643
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