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Glycosylatable GFP as a compartment-specific membrane topology reporter
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
2012 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 427, no 4, 780-784 p.Article in journal (Refereed) Published
Abstract [en]

Determination of the membrane topology is an essential step in structural and functional studies of integral membrane proteins, yet the choices of membrane topology reporters are limited and the experimental analysis can be laborious, especially in eukaryotic cells. Here, we present a robust membrane topology reporter, glycosylatable green fluorescent protein (gGFP). gGFP is fully fluorescent in the yeast cytosol but becomes glycosylated and does not fluoresce in the lumen of the endoplasmic reticulum (ER). Thus, by assaying fluorescence and the glycosylation status of C-terminal fusions of gGFP to target membrane proteins in whole-cell lysates, the localization of the gGFP moiety (and hence the fusion joint) relative to the ER membrane can be unambiguously determined.

Place, publisher, year, edition, pages
2012. Vol. 427, no 4, 780-784 p.
Keyword [en]
GFP, Membrane topology, N-linked glycosylation, Saccharomyces cerevisiae, Yeast
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-83804DOI: 10.1016/j.bbrc.2012.09.138ISI: 000311134700017OAI: diva2:577160


Available from: 2012-12-14 Created: 2012-12-14 Last updated: 2012-12-14Bibliographically approved

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von Heijne, Gunnar
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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