Polyisoprenol Specificity in the Campylobacter jejuni N-Linked Glycosylation Pathway: Biochemistry

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TypeArticle
Journal titleBiochemistry
Volume46
Issue50
Pages1434214348; # of pages: 7
Subjectanalysis; Asparagine; Biochemistry; Biochemistry And Biophysics; BOND; Campylobacter; Campylobacter jejuni; Canada; CHAIN; chemistry; COMPONENT; ENZYME; enzymes; Glycosylation; kinetic; membrane; N-linked; PATHWAY; POTENTIAL; protein; Role; SPECIFICITY; Substrate Specificity; SUBSTRATE-SPECIFICITY; SUBSTRATES; SYSTEM; transferred
AbstractCampylobacter jejuni contains a general N-linked glycosylation pathway in which a heptasaccharide is sequentially assembled onto a polyisoprenyl diphosphate carrier and subsequently transferred to the asparagine side chain of an acceptor protein. The enzymes in the pathway function at a membrane interface and have in common amphiphilic membrane-bound polyisoprenyl-linked substrates. Herein, we examine the potential role of the polyisoprene component of the substrates by investigating the relative substrate efficiencies of polyisoprene-modified analogues in individual steps of the pathway. Chemically defined substrates for PglC, PglJ, and PglB are prepared via semisynthetic approaches. The substrates included polyisoprenols of varying length, double bond geometry, and degree of saturation for probing the role of the hydrophobic polyisoprene in substrate specificity. Kinetic analysis reveals that all three enzymes exhibit distinct preferences for the polyisoprenyl carrier whereby cis-double bond geometry and alpha-unsaturation of the native substrate are important features, while the precise polyisoprene length may be less critical. These findings suggest that the polyisoprenyl carrier plays a specific role in the function of these enzymes beyond a purely physical role as a membrane anchor. These studies underscore the potential of the C. jejuni N-linked glycosylation pathway as a system for investigating the biochemical and biophysical roles of polyisoprenyl carriers common to prokaryotic and eukaryotic glycosylation
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberCHEN2007A
NPARC number9378335
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Record identifier65cb703f-d81c-43aa-832c-946629e895fe
Record created2009-07-10
Record modified2016-05-09
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