Active membrane transport and receptor proteins from bacteria
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review
Author(s)
Detail(s)
Original language | English |
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Pages (from-to) | 867-872 |
Journal / Publication | Biochemical Society Transactions |
Volume | 33 |
Issue number | 4 |
Publication status | Published - Aug 2005 |
Externally published | Yes |
Link(s)
Abstract
A general strategy for the expression of bacterial membrane transport and receptor genes in Escherichia coli is described. Expression is amplified so that the encoded proteins comprise 5-35% of E. coli inner membrane protein. Depending upon their topology, proteins are produced with RGSH6 or a Strep tag at the C-terminus. These enable purification in mg quantities for crystallization and NMR studies. Examples of one nutrient uptake and one multidrug extrusion protein from Helicobacter pylori are described. This strategy is successful for membrane proteins from H. pylori, E. coli, Enterococcus faecalis, Bacillus subtilis, Staphylococcus aureus, Microbacterium liquefaciens, Brucella abortus, Brucella melitensis, Campylobacter jejuni, Neisseria meningitides, Streptomyces coelicolor and Rhodobacter sphaeroides. ©2005 Biochemical Society.
Research Area(s)
- Bacteria, Helicobacter pylori, His tag, Membrane transport protein, Pathogen, Two-component system
Bibliographic Note
Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].
Citation Format(s)
Active membrane transport and receptor proteins from bacteria. / Saidijam, M.; Bettaney, K. E.; Szakonyi, G. et al.
In: Biochemical Society Transactions, Vol. 33, No. 4, 08.2005, p. 867-872.
In: Biochemical Society Transactions, Vol. 33, No. 4, 08.2005, p. 867-872.
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review