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Confronting fusion protein-based membrane protein topology mapping with reality: the Escherichia coli ClcA H+/Cl- exchange transporter.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2008 (English)In: J Mol Biol, ISSN 1089-8638, Vol. 381, no 4, 860-6 p.Article in journal (Refereed) Published
Abstract [en]

The topology of bacterial inner membrane proteins is commonly determined using topology reporters such as alkaline phosphatase and green fluorescent protein fused to a series of C-terminally truncated versions of the protein in question. Here, we report a detailed topology mapping of the Escherichia coli inner membrane H(+)/Cl(-) exchange transporter ClcA. Since the 3-D structure of ClcA is known, our results provide a critical test of the reporter fusion approach and offer new insights into the ClcA folding pathway.

Place, publisher, year, edition, pages
2008. Vol. 381, no 4, 860-6 p.
Keyword [en]
Alkaline Phosphatase/metabolism, Amino Acid Sequence, Antiporters/chemistry/*metabolism, Escherichia coli/*metabolism, Escherichia coli Proteins/chemistry/*metabolism, Genes; Reporter, Green Fluorescent Proteins/metabolism, Ion Pumps/*metabolism, Membrane Proteins/*metabolism, Models; Molecular, Molecular Sequence Data, Protein Structure; Secondary, Recombinant Fusion Proteins/*metabolism
Identifiers
URN: urn:nbn:se:su:diva-14919ISI: 000258971300006PubMedID: 18590742OAI: oai:DiVA.org:su-14919DiVA: diva2:181439
Available from: 2009-01-23 Created: 2009-01-23 Last updated: 2011-01-10Bibliographically approved

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Seppälä, Susannavon Heijne, Gunnar
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