title: Protein glycosylation in Campylobacter jejuni: partial suppression of pglF by mutation of pseC.
abstract: Campylobacter jejuni has systems for N- and O-linked protein glycosylation. Although biochemical evidence demonstrated that a pseC mutant in the O-linked pathway accumulated the product of pglF in the N-linked pathway, analyses of transformation frequencies and glycosylation statuses of N-glycosylated proteins indicated a partial suppression of pglF by pseC.
authors.affiliation: Enteric Diseases Department, Naval Medical Research Center, 503 Robert Grant Ave., Silver Spring, MD 20910, USA. guerryp@nmrc.navy.mil
authors.forename: Patricia
authors.initials: P
authors.lastname: Guerry
authors.forename: Cheryl P
authors.initials: CP
authors.lastname: Ewing
authors.forename: Ian C
authors.initials: IC
authors.lastname: Schoenhofen
authors.forename: Susan M
authors.initials: SM
authors.lastname: Logan
mesh_terms: D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000096:biosynthesis; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D016123:Campylobacter jejuni / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006031:Glycosylation; D006836:Hydro-Lyases / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D012794:Sialic Acids / Q000096:biosynthesis; D000637:Transaminases / Q000235:genetics* / Q000378:metabolism; D014169:Transformation, Bacterial
chemical_list: C502751:2,4-diacetamido-2,4,6-trideoxyglucopyranose; C502287:5,7-diacetamido-3,5,7,9-tetradeoxynon-2-ulosonic acid; D001426:Bacterial Proteins; D012794:Sialic Acids; D000637:Transaminases; D006836:Hydro-Lyases; D000117:Acetylglucosamine