Document Detail


An engineered eukaryotic protein glycosylation pathway in Escherichia coli.
MedLine Citation:
PMID:  22446837     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We performed bottom-up engineering of a synthetic pathway in Escherichia coli for the production of eukaryotic trimannosyl chitobiose glycans and the transfer of these glycans to specific asparagine residues in target proteins. The glycan biosynthesis was enabled by four eukaryotic glycosyltransferases, including the yeast uridine diphosphate-N-acetylglucosamine transferases Alg13 and Alg14 and the mannosyltransferases Alg1 and Alg2. By including the bacterial oligosaccharyltransferase PglB from Campylobacter jejuni, we successfully transferred glycans to eukaryotic proteins.
Authors:
Juan D Valderrama-Rincon; Adam C Fisher; Judith H Merritt; Yao-Yun Fan; Craig A Reading; Krishan Chhiba; Christian Heiss; Parastoo Azadi; Markus Aebi; Matthew P DeLisa
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-03-25
Journal Detail:
Title:  Nature chemical biology     Volume:  8     ISSN:  1552-4469     ISO Abbreviation:  Nat. Chem. Biol.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-04-18     Completed Date:  2012-06-29     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  101231976     Medline TA:  Nat Chem Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  434-6     Citation Subset:  IM    
Affiliation:
School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA.
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MeSH Terms
Descriptor/Qualifier:
Campylobacter jejuni / enzymology
Disaccharides / biosynthesis*
Escherichia coli / metabolism*
Escherichia coli Proteins / metabolism*
Glycosylation
Hexosyltransferases / metabolism
Mannosyltransferases / metabolism
Membrane Proteins / metabolism
N-Acetylglucosaminyltransferases / metabolism
Polysaccharides / biosynthesis*
Protein Engineering*
Saccharomyces cerevisiae Proteins / metabolism
Grant Support
ID/Acronym/Agency:
1 P41 RR018502-01/RR/NCRR NIH HHS; R43 GM086965/GM/NIGMS NIH HHS; R43 GM086965/GM/NIGMS NIH HHS; R43 GM087766/GM/NIGMS NIH HHS; R43 GM087766/GM/NIGMS NIH HHS; R43 GM088905/GM/NIGMS NIH HHS; R44 GM088905/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Disaccharides; 0/Escherichia coli Proteins; 0/Membrane Proteins; 0/Polysaccharides; 0/Saccharomyces cerevisiae Proteins; 577-76-4/chitobiose; EC 2.4.1.-/ALG2 protein, S cerevisiae; EC 2.4.1.-/Alg13 protein, S cerevisiae; EC 2.4.1.-/Alg14 protein, S cerevisiae; EC 2.4.1.-/Hexosyltransferases; EC 2.4.1.-/Mannosyltransferases; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC 2.4.1.119/dolichyl-diphosphooligosaccharide - protein glycotransferase; EC 2.4.1.142/chitobiosyldiphosphodolichol beta-mannosyltransferase
Comments/Corrections

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