Improving the soluble expression of aequorin in Escherichia coli using the chaperone-based approach by co-expression with artemin

References

• Fink, A.L. Protein Aggregation: Folding Aggregates, Inclusion Bodies and Amyloid. Fold. Des. 1998, 3, R9–R23.
   PubMedGoogle Scholar
• Mitraki, A.; Haase-Pettingell, C.; King, J. Mechanisms of Inclusion Body Formation. ACS Publications, Washington, DC, USA, 1991, 35–49.
   Google Scholar
• Wetzel, R. For Protein Misassembly, it’s the “I” decade. Cell. 1996, 86, 699–702.
   PubMed Web of Science ®Google Scholar
• Wang, W. Protein Aggregation and Its Inhibition in Biopharmaceutics. Int. J. Pharm. 2005, 289, 1–30.
   PubMed Web of Science ®Google Scholar
• Fink, A.L. Chaperone-Mediated Protein Folding. Physiol. Rev. 1999, 79, 425–449.
   PubMed Web of Science ®Google Scholar
• Kumar, S.; Jain, K.K.; Bhardwaj, K.N.; Chakraborty, S.; Kuhad, R.C. Multiple Genes in a Single Host: Cost-Effective Production of Bacterial Laccase (cotA), Pectate Lyase (Pel), and Endoxylanase (Xyl) by Simultaneous Expression and Cloning in Single Vector in Escherichia coli. PLoS One. 2015, 10, e0144379.
   PubMed Web of Science ®Google Scholar
• Fahnert, B. Using Folding Promoting Agents in Recombinant Protein Production: A Review. Recomb. Gene Expr. 2012, 824, 3–36.
   Google Scholar
• de Marco, A.; Deuerling, E.; Mogk, A.; Tomoyasu, T.; Bukau, B. Chaperone-Based Procedure to Increase Yields of Soluble Recombinant Proteins Produced in Escherichia coli. BMC Biotechnol. 2007, 7, 32.
   PubMed Web of Science ®Google Scholar
• Gragerov, A.; Nudler, E.; Komissarova, N.; Gaitanaris, G.A.; Gottesman, M.E.; Nikiforov, V. Cooperation of GroEL/GroES and DnaK/DnaJ Heat Shock Proteins in Preventing Protein Misfolding in Escherichia coli. Proc. Natl. Acad. Sci. USA. 1992, 89, 10341–10344.
   PubMed Web of Science ®Google Scholar
• Sørensen, H.P.; Mortensen, K.K. Soluble Expression of Recombinant Proteins in the Cytoplasm of Escherichia coli. Microb. Cell Fact. 2005, 4, 1.
   PubMed Web of Science ®Google Scholar
• Alibolandi, M.; Mirzahoseini, H.; Moshtaghi Nehi, F.; Tabatabaian, G.; Amini, H.; Sardari, S. Improving Recombinant Protein Solubility in Escherichia coli: Identification of Best Chaperone Combination Which Assists Folding of Human Basic Fibroblast Growth Factor. African J. Biotechnol. 2010, 9, 8100–8109.
   Google Scholar
• Baneyx, F.; Mujacic, M. Recombinant Protein Folding and Misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399–1408.
   PubMed Web of Science ®Google Scholar
• Jalilian, N.; Shanehsaz, M.; Sajedi, R.H.; Gharaat, M.; Ghahremanzadeh, R. Improving the Luminescence Properties of Aequorin by Conjugating to CdSe/ZnS Quantum Dot Nanoparticles: Red Shift and Slowing Decay Rate. J. Photochem. Photobiol. B Biol. 2016, 162, 153–161.
   PubMed Web of Science ®Google Scholar
• Jalilian, N.; Sajedi, R.H.; Shanehsaz, M.; Gharaat, M. CdTe Quantum Dots with Green Fluorescence Generated by Bioluminescence Resonance Energy Transfer from Aequorin. Microchim. Acta. 2017, 184, 753–762.
   Web of Science ®Google Scholar
• Zeinoddini, M.; Khajeh, K.; Hosseinkhani, S.; Saeedinia, A.R.; Robatjazi, S.M. Stabilisation of Recombinant Aequorin by Polyols: Activity, Thermostability and Limited Proteolysis. Appl. Biochem. Biotechnol. 2013, 170, 273–280.
   PubMed Web of Science ®Google Scholar
• Takalloo, Z.; Sajedi, R.H.; Hosseinkhani, S.; Asghari, S.M. Real-Time Monitoring of Artemin In Vivo Chaperone Activity Using Luciferase as an Intracellular Reporter. Arch. Biochem. Biophys. 2016, 610, 33–40.
   PubMed Web of Science ®Google Scholar
• Takalloo, Z.; Sajedi, R.H.; Hosseinkhani, S.; Moazzenzade, T. Artemin Protects Cells and Proteins against Oxidative and Salt Stress. Int. J. Biol. Macromol. 2017, 95, 618–624.
   PubMed Web of Science ®Google Scholar
• Shirzad, F.; Sajedi, R.H.; Shahangian, S.S.; Rasti, B.; Mosadegh, B.; Taghdir, M.; Hosseinkhani, S. Deletion of Extra C-Terminal Segment and Its Effect on the Function and Structure of Artemin. Int. J. Biol. Macromol. 2011, 49, 311–316.
   PubMed Web of Science ®Google Scholar
• Shahangian, S.S.; Rasti, B.; Sajedi, R.H.; Khodarahmi, R.; Taghdir, M.; Ranjbar, B. Artemin as an Efficient Molecular Chaperone. Protein J. 2011, 30, 549–557.
   PubMed Web of Science ®Google Scholar
• Grinstead, K.M.; Rowe, L.; Ensor, C.M.; Joel, S.; Daftarian, P.; Dikici, E.; Zingg, J.M.; Daunert, S. Red-Shifted Aequorin Variants Incorporating Non-Canonical Amino Acids: Applications in In Vivo Imaging. PLoS One. 2016, 11, e0158579.
   PubMed Web of Science ®Google Scholar
• Cormier, M.J.; Prasher, D.C.; Longiaru, M.; Mccann, R.O. The Enzymology and Molecular Biology of the Ca2+-Activated Photoprotein, Aequorin. Photochem. Photobiol. 1989, 49, 509–512.
   PubMed Web of Science ®Google Scholar
• Shimomura, O.; Inouye, S. The In Situ Regeneration and Extraction of Recombinant Aequorin from Escherichia coli Cells and the Purification of Extracted Aequorin. Protein Expr. Purif. 1999, 16, 91–95.
   PubMed Web of Science ®Google Scholar
• Inouye, S.; Aoyama, S.; Miyata, T.; Tsuji, F.I.; Sakaki, Y. Overexpression and purification of the recombinant Ca2+-binding protein, apoaequorin. J. Biochem. 1989, 105, 473–477.
   PubMed Web of Science ®Google Scholar
• Laemmli, U.K. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature. 1970, 227, 680–685.
   PubMed Web of Science ®Google Scholar
• Bradford, M.M. A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding. Anal. Biochem. 1976, 72, 248–254.
   PubMed Web of Science ®Google Scholar
• De Marco, A. Strategies for Successful Recombinant Expression of Disulfide Bond-Dependent Proteins in Escherichia coli. Microb. Cell Fact. 2009, 8, 26.
   PubMed Web of Science ®Google Scholar
• Cabrita, L.D.; Dai, W.; Bottomley, S.P. A Family of Escherichia coli Expression Vectors for Laboratory Scale and High Throughput Soluble Protein Production. BMC Biotechnol. 2006, 6, 12.
   PubMed Web of Science ®Google Scholar
• Ikura, K.; Kokubu, T.; Natsuka, S.; Ichikawa, A.; Adachi, M.; Nishihara, K.; Yanagi, H.; Utsumi, S. Co-Overexpression of Folding Modulators Improves the Solubility of the Recombinant guinea Pig Liver Transglutaminase Expressed in Escherichia coli. Prep. Biochem. Biotechnol. 2002, 32, 189–205.
   PubMed Web of Science ®Google Scholar
• Romier, C.; Ben Jelloul, M.; Albeck, S.; Buchwald, G.; Busso, D.; Celie, P.H.N.; Christodoulou, E.; De Marco, V.; van Gerwen, S.; Knipscheer, P.; et al. Co-Expression of Protein Complexes in Prokaryotic and Eukaryotic Hosts: Experimental Procedures, Database Tracking and Case Studies. Acta Crystallogr. D Biol. Crystallogr. 2006, 62, 1232–1242.
   PubMedGoogle Scholar
• Wladyka, B.; Puzia, K.; Dubin, A. Efficient Co-expression of a Recombinant Staphopain A and Its Inhibitor Staphostatin A in Escherichia coli. Biochem. J. 2005, 385, 181–187.
   PubMed Web of Science ®Google Scholar
• Goyal, M.; Chaudhuri, T.K. GroEL–GroES Assisted Folding of Multiple Recombinant Proteins Simultaneously over-Expressed in Escherichia coli. Int. J. Biochem. Cell Biol. 2015, 64, 277–286.
   PubMed Web of Science ®Google Scholar
• Jones, H.E.; Holland, I.B.; Baker, H.L.; Campbell, A.K. Slow Changes in Cytosolic Free Ca2+ in Escherichia coli Highlight Two Putative Influx Mechanisms in Response to Changes in Extracellular Calcium. Cell Calcium. 1999, 25, 265–274.
   PubMed Web of Science ®Google Scholar
• Knight, M.R.; Campbell, A.K.; Smith, S.M.; Trewavas, A.J. Recombinant Aequorin as a Probe for Cytosolic Free Ca2+ in Escherichia coli. FEBS Lett. 1991, 282, 405–408.
   PubMed Web of Science ®Google Scholar
• Guragain, M.; Campbell, A.K.; Patrauchan, M.A. Measurement of Intracellular Calcium Concentration in Pseudomonas aeruginosa. J. Bacteriol. 2016, 6, 3.
   Google Scholar
• Nelson, G.; Kozlova-Zwinderman, O.; Collis, A.J.; Knight, M.R.; Fincham, J.R.S.; Stanger, C.P.; Renwick, A.; Hessing, J.G.M.; Punt, P.J.; Van Den Hondel, C.A.M.J.J.; Read, N.D. Calcium Measurement in Living Filamentous Fungi Expressing Codon‐Optimized Aequorin. Mol. Microbiol. 2004, 52, 1437–1450.
   PubMed Web of Science ®Google Scholar
• González, M.N.; Villaverde, A.; Aris, A. Amyloid-Linked Cellular Toxicity Triggered by Bacterial Inclusion Bodies. Biochem. Biophys. Res. Commun. 2007, 355, 637–642.
   PubMed Web of Science ®Google Scholar