Publication Date:
2002-12-03
Description:
N-linked protein glycosylation is the most abundant posttranslation modification of secretory proteins in eukaryotes. A wide range of functions are attributed to glycan structures covalently linked to asparagine residues within the asparagine-X-serine/threonine consensus sequence (Asn-Xaa-Ser/Thr). We found an N-linked glycosylation system in the bacterium Campylobacter jejuni and demonstrate that a functional N-linked glycosylation pathway could be transferred into Escherichia coli. Although the bacterial N-glycan differs structurally from its eukaryotic counterparts, the cloning of a universal N-linked glycosylation cassette in E. coli opens up the possibility of engineering permutations of recombinant glycan structures for research and industrial applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wacker, Michael -- Linton, Dennis -- Hitchen, Paul G -- Nita-Lazar, Mihai -- Haslam, Stuart M -- North, Simon J -- Panico, Maria -- Morris, Howard R -- Dell, Anne -- Wren, Brendan W -- Aebi, Markus -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1790-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zurich, CH-8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459590" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/chemistry/genetics/isolation & purification/*metabolism
;
Campylobacter jejuni/genetics/*metabolism
;
Carbohydrate Conformation
;
*Cloning, Molecular
;
Conjugation, Genetic
;
Consensus Sequence
;
Escherichia coli/*genetics/metabolism
;
*Escherichia coli Proteins
;
Genes, Bacterial
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Genetic Complementation Test
;
Glycoproteins/chemistry/*metabolism
;
Glycosylation
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Glycosyltransferases/genetics/metabolism
;
Lipoproteins/genetics/isolation & purification/metabolism
;
Mass Spectrometry
;
Membrane Transport Proteins
;
Models, Biological
;
Mutation
;
Polysaccharides, Bacterial/biosynthesis
;
Recombinant Proteins/chemistry/isolation & purification
;
Transformation, Bacterial
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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