Active membrane transport and receptor proteins from bacteria

M. Saidijam; K.E. Bettaney; G. Szakonyi; G. Psakis; K. Shibayama; S. Suzuki; J.L. Clough; V. Blessie; A. Abu-bakr; S. Baumberg; J. Meuller; C.K. Hoyle; S.L. Palmer; P. Butaye; K. Walravens; S.G. Patching; J. O'Reilly; NG. Rutherford; Roslyn M. Bill; D.I. Roper; M.K. Phillips-Jones; P.J.F. Henderson

doi:10.1042/BST0330867

Active membrane transport and receptor proteins from bacteria

M. Saidijam, K.E. Bettaney, G. Szakonyi, G. Psakis, K. Shibayama, S. Suzuki, J.L. Clough, V. Blessie, A. Abu-bakr, S. Baumberg, J. Meuller, C.K. Hoyle, S.L. Palmer, P. Butaye, K. Walravens, S.G. Patching, J. O'Reilly, NG. Rutherford, Roslyn M. Bill, D.I. RoperM.K. Phillips-Jones, P.J.F. Henderson

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	867-872
Number of pages	6
Journal	Biochemical Society Transactions
Volume	33
Issue number	Part 4
DOIs	https://doi.org/10.1042/BST0330867
Publication status	Published - Aug 2005

Bibliographical note

Copyright 2005 The Biochemical Society. The Accepted Manuscript is reproduced here in accordance with the copyright policy of the publisher. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Portland Press Limited. The final Version of Record is available at http://www.biochemsoctrans.org Conference on Mechanisms of Bioenergetic Membrane Proteins - Structures and Beyond, Wiesbaden (DE), 20-24 March 2005

Keywords

bacteria
helicobacter pylori
his tag
membrane transport protein
pathogen
two-component system

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10.1042/BST0330867

Active membrane transport and receptor proteins from bacteria
Copyright 2005 The Biochemical Society. The Accepted Manuscript is reproduced here in accordance with the copyright policy of the publisher. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Portland Press Limited. The final Version of Record is available at http://www.biochemsoctrans.org Conference on Mechanisms of Bioenergetic Membrane Proteins - Structures and Beyond, Wiesbaden (DE), 20-24 March 2005
Accepted author manuscript, 847 KB

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Saidijam, M., Bettaney, K. E., Szakonyi, G., Psakis, G., Shibayama, K., Suzuki, S., Clough, J. L., Blessie, V., Abu-bakr, A., Baumberg, S., Meuller, J., Hoyle, C. K., Palmer, S. L., Butaye, P., Walravens, K., Patching, S. G., O'Reilly, J., Rutherford, NG., Bill, R. M., ... Henderson, P. J. F. (2005). Active membrane transport and receptor proteins from bacteria. Biochemical Society Transactions, 33(Part 4), 867-872. https://doi.org/10.1042/BST0330867

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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. {\textcopyright}2005 Biochemical Society.",

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note = "Copyright 2005 The Biochemical Society. The Accepted Manuscript is reproduced here in accordance with the copyright policy of the publisher. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Portland Press Limited. The final Version of Record is available at http://www.biochemsoctrans.org Conference on Mechanisms of Bioenergetic Membrane Proteins - Structures and Beyond, Wiesbaden (DE), 20-24 March 2005",

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Saidijam, M, Bettaney, KE, Szakonyi, G, Psakis, G, Shibayama, K, Suzuki, S, Clough, JL, Blessie, V, Abu-bakr, A, Baumberg, S, Meuller, J, Hoyle, CK, Palmer, SL, Butaye, P, Walravens, K, Patching, SG, O'Reilly, J, Rutherford, NG, Bill, RM, Roper, DI, Phillips-Jones, MK & Henderson, PJF 2005, 'Active membrane transport and receptor proteins from bacteria', Biochemical Society Transactions, vol. 33, no. Part 4, pp. 867-872. https://doi.org/10.1042/BST0330867

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T1 - Active membrane transport and receptor proteins from bacteria

AU - Saidijam, M.

AU - Bettaney, K.E.

AU - Szakonyi, G.

AU - Psakis, G.

AU - Shibayama, K.

AU - Suzuki, S.

AU - Clough, J.L.

AU - Blessie, V.

AU - Abu-bakr, A.

AU - Baumberg, S.

AU - Meuller, J.

AU - Hoyle, C.K.

AU - Palmer, S.L.

AU - Butaye, P.

AU - Walravens, K.

AU - Patching, S.G.

AU - O'Reilly, J.

AU - Rutherford, NG.

AU - Bill, Roslyn M.

AU - Roper, D.I.

AU - Phillips-Jones, M.K.

AU - Henderson, P.J.F.

N1 - Copyright 2005 The Biochemical Society. The Accepted Manuscript is reproduced here in accordance with the copyright policy of the publisher. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Portland Press Limited. The final Version of Record is available at http://www.biochemsoctrans.org Conference on Mechanisms of Bioenergetic Membrane Proteins - Structures and Beyond, Wiesbaden (DE), 20-24 March 2005

PY - 2005/8

Y1 - 2005/8

N2 - 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.

AB - 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.

KW - bacteria

KW - helicobacter pylori

KW - his tag

KW - membrane transport protein

KW - pathogen

KW - two-component system

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U2 - 10.1042/BST0330867

DO - 10.1042/BST0330867

M3 - Article

C2 - 16042616

SN - 0300-5127

VL - 33

SP - 867

EP - 872

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - Part 4

ER -

Active membrane transport and receptor proteins from bacteria

Abstract

Bibliographical note

Keywords

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