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. 2007 May;2(2):73-81.
doi: 10.1155/2006/510578.

An analysis of amino acid sequences surrounding archaeal glycoprotein sequons

Mehtap Abu-Qarn  1 , Jerry Eichler
Affiliations

An analysis of amino acid sequences surrounding archaeal glycoprotein sequons

Mehtap Abu-Qarn et al. Archaea. 2007 May.

Abstract

Despite having provided the first example of a prokaryal glycoprotein, little is known of the rules governing the N-glycosylation process in Archaea. As in Eukarya and Bacteria, archaeal N-glycosylation takes place at the Asn residues of Asn-X-Ser/Thr sequons. Since not all sequons are utilized, it is clear that other factors, including the context in which a sequon exists, affect glycosylation efficiency. As yet, the contribution to N-glycosylation made by sequon-bordering residues and other related factors in Archaea remains unaddressed. In the following, the surroundings of Asn residues confirmed by experiment as modified were analyzed in an attempt to define sequence rules and requirements for archaeal N-glycosylation.

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Figures

Figure 1.
Figure 1.
Analysis of the characteristics of amino acids surrounding modified Asn residues in archaeal glycoproteins. The relative proportions of acidic (DE), basic (KRH), polar uncharged (NQSTY) and polar (AVLIPFMWGC) residues were considered at 10 positions up- and downstream of modified archaeal NXS (upper panel, based on 14 sequences) and NXT (lower panel, based on 13 sequences) sequons. In each case, the character of the residue at the X position was also considered. In each panel, the positions of the modified Asn as well as the sequon Ser (upper panel) or Thr (lower panel) are indicated.
See this image and copyright information in PMC

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