Production of Membrane Proteins in Pseudomonas stutzeri.
Arabinose induction
Membrane protein
Protein overexpression
Pseudomonas stutzeri
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
30
6
2022
pubmed:
1
7
2022
medline:
6
7
2022
Statut:
ppublish
Résumé
Functional and structural studies on membrane proteins are often hampered by insufficient yields, misfolding and aggregation during the production and purification process. Escherichia coli is the most commonly used expression host for the production of recombinant prokaryotic integral membrane proteins. However, in many cases expression hosts other than E. coli are more appropriate for certain target proteins. Here, we report a convenient, systematically developed expression system using the γ-proteobacterium Pseudomonas stutzeri as an alternative production host for over-expression of integral membrane proteins. P. stutzeri can be easily and inexpensively cultured in large quantities. The Pseudomonas expression vectors are designed for inducible expression of affinity-tagged fusion proteins controlled by the P
Identifiants
pubmed: 35773579
doi: 10.1007/978-1-0716-2368-8_6
doi:
Substances chimiques
Membrane Proteins
0
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
91-110Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Terpe K (2006) Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 72:211–222
doi: 10.1007/s00253-006-0465-8
Chen R (2012) Bacterial expression systems for recombinant protein production: E. coli and beyond. Biotechnol Adv 30:1102–1107
doi: 10.1016/j.biotechadv.2011.09.013
Demain AL, Vaishnav P (2009) Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27:297–306
doi: 10.1016/j.biotechadv.2009.01.008
Zweers JC, Barák I, Becher D, Driessen AJ, Hecker M, Kontinen VP, Saller MJ, Vavrová L, van Dijl JM (2008) Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes. Microb Cell Factories 7:10
doi: 10.1186/1475-2859-7-10
Retallack DM, Jin H, Chew L (2012) Reliable protein production in a Pseudomonas fluorescens expression system. Protein Expr Purif 81:157–165
doi: 10.1016/j.pep.2011.09.010
Kunji ERS, Slotboom D-J, Poolman B (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim Biophys Acta 1610:97–108
doi: 10.1016/S0005-2736(02)00712-5
Funes S, Hasona A, Bauerschmitt H, Grubbauer C, Kauff F, Collins R, Crowley PJ, Palmer SR, Brady LJ, Herrmann JM (2009) Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function. Proc Natl Acad Sci U S A 106:6656–6661
doi: 10.1073/pnas.0809951106
Sommer M, Xie H, Michel H (2017) Pseudomonas stutzeri as an alternative host for membrane proteins. Microb Cell Factories 16:157
doi: 10.1186/s12934-017-0771-0
Lalucat J, Bennasar A, Bosch R, Garcia-Valdes E, Palleroni N (2006) Biology of Pseudomonas stutzeri. Microbiol Mol Biol Rev 70:510–547
doi: 10.1128/MMBR.00047-05
Kovach ME, Elzer PH, Hill DS, Robertson GT, Farris MA, Roop RM, Peterson KM (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175–176
doi: 10.1016/0378-1119(95)00584-1
Kovach ME, Phillips RW, Elzer PH, Roop RM, Peterson KM (1994) pBBR1MCS: a broad-host-range cloning vector. BioTechniques 16:800–802
pubmed: 8068328
Geertsma ER, Groeneveld M, Slotboom D-J, Poolman B (2008) Quality control of overexpressed membrane proteins. Proc Natl Acad Sci U S A 105:5722–5727
doi: 10.1073/pnas.0802190105
Tropea JE, Cherry S, Waugh DS (2009) Expression and purification of soluble His(6)-tagged TEV protease. Methods Mol Biol 498:297–307
doi: 10.1007/978-1-59745-196-3_19
Zacharias DA, Violin JD, Newton AC, Tsien RY (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296:913–916
doi: 10.1126/science.1068539
Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ (2000) Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol 182:4068–4076
doi: 10.1128/JB.182.14.4068-4076.2000
Aslanidis C, de Jong PJ (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18:6069–6074
doi: 10.1093/nar/18.20.6069
Li MZ, Elledge SJ (2007) Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC. Nat Methods 4:251–256
doi: 10.1038/nmeth1010