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N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase

(2006) SCIENCE. 314(5802). p.1148-1150
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Abstract
N-linked protein glycosylation is found in all domains of life. In eukaryotes, it is the most abundant protein modification of secretory and membrane proteins, and the process is coupled to protein translocation and folding. We found that in bacteria, N-glycosylation can occur independently of the protein translocation machinery. In an in vitro assay, bacterial oligosaccharyltransferase glycosylated a folded endogenous substrate protein with high efficiency and folded bovine ribonuclease A with low efficiency. Unfolding the eukaryotic substrate greatly increased glycosylation. We propose that in the bacterial system, glycosylation sites are located in flexible parts of folded proteins, whereas the eukaryotic cotranslational glycosylation evolved to a mechanism presenting the substrate in a flexible form before folding.
Keywords
CAMPYLOBACTER-JEJUNI, TAT PATHWAY, ESCHERICHIA-COLI, TRANSLOCATION, COMPLEX, ENDOPLASMIC-RETICULUM, GREEN FLUORESCENT PROTEIN, TRANSFERASE, SPECIFICITY, RECOGNITION

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Chicago
Kowarik, Michael, Shin Numao, Mario F Feldman, Benjamin L Schulz, Nico Callewaert, Eva Kiermaier, Ina Catrein, and Markus Aebi. 2006. “N-linked Glycosylation of Folded Proteins by the Bacterial Oligosaccharyltransferase.” Science 314 (5802): 1148–1150.
APA
Kowarik, M., Numao, S., Feldman, M. F., Schulz, B. L., Callewaert, N., Kiermaier, E., Catrein, I., et al. (2006). N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. SCIENCE, 314(5802), 1148–1150.
Vancouver
1.
Kowarik M, Numao S, Feldman MF, Schulz BL, Callewaert N, Kiermaier E, et al. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. SCIENCE. 2006;314(5802):1148–50.
MLA
Kowarik, Michael, Shin Numao, Mario F Feldman, et al. “N-linked Glycosylation of Folded Proteins by the Bacterial Oligosaccharyltransferase.” SCIENCE 314.5802 (2006): 1148–1150. Print.
@article{1203449,
  abstract     = {N-linked protein glycosylation is found in all domains of life. In eukaryotes, it is the most abundant protein modification of secretory and membrane proteins, and the process is coupled to protein translocation and folding. We found that in bacteria, N-glycosylation can occur independently of the protein translocation machinery. In an in vitro assay, bacterial oligosaccharyltransferase glycosylated a folded endogenous substrate protein with high efficiency and folded bovine ribonuclease A with low efficiency. Unfolding the eukaryotic substrate greatly increased glycosylation. We propose that in the bacterial system, glycosylation sites are located in flexible parts of folded proteins, whereas the eukaryotic cotranslational glycosylation evolved to a mechanism presenting the substrate in a flexible form before folding.},
  author       = {Kowarik, Michael and Numao, Shin and Feldman, Mario F and Schulz, Benjamin L and Callewaert, Nico and Kiermaier, Eva and Catrein, Ina and Aebi, Markus},
  issn         = {0036-8075},
  journal      = {SCIENCE},
  keyword      = {CAMPYLOBACTER-JEJUNI,TAT PATHWAY,ESCHERICHIA-COLI,TRANSLOCATION,COMPLEX,ENDOPLASMIC-RETICULUM,GREEN FLUORESCENT PROTEIN,TRANSFERASE,SPECIFICITY,RECOGNITION},
  language     = {eng},
  number       = {5802},
  pages        = {1148--1150},
  title        = {N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase},
  url          = {http://dx.doi.org/10.1126/science.1134351},
  volume       = {314},
  year         = {2006},
}

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