Browse > Article
http://dx.doi.org/10.4014/mbl.1808.08001

Recombinant Protein Disulfide Isomerase A3 with an Elongated Peptide Tag Production Process Using Escherichia coli  

Kim, Kwang-Jin (Department of Pharmacy, Sunchon National University)
You, Sung-Hwan (Department of Biological Sciences, College of Natural Sciences, Chonnam National University)
Lee, Yongjin (Department of Pharmacy, Sunchon National University)
Park, Chan Mi (Department of Oral Biochemistry, Dental Science Research Institute, School of Dentistry, Chonnam National University)
Kim, Geun-Joong (Department of Biological Sciences, College of Natural Sciences, Chonnam National University)
Lee, Tae-Hoon (Department of Oral Biochemistry, Dental Science Research Institute, School of Dentistry, Chonnam National University)
Son, Young-Jin (Department of Pharmacy, Sunchon National University)
Publication Information
Microbiology and Biotechnology Letters / v.46, no.3, 2018 , pp. 244-252 More about this Journal
Abstract
Protein disulfide isomerase A3 (PDIA3) is a major member of the protein disulfide isomerase (PDI) family. PDI proteins commonly reside in the endoplasmic reticulum and mediate important thiol-disulfide interchanges during post-translational protein folding. Unlike other PDI family members, PDIA3 is ubiquitous in various organ systems. However, its physiological activity varies in other tissues. PDIA3 has been associated with cancer, airway inflammation, neurodegenerative diseases, and metabolic diseases. However, the mechanisms of the association of PDIA3 with these pathological conditions remain unclear. Recombinant PDIA3 (rPDIA3) is needed to clarify the interactions between PDIA3 and certain physiological phenomena. In the present study, we aimed to produce highly purified rPDIA3 for use in pathological experiments. We expressed rPDIA3 with a histidine-enriched elongated peptide tag in Escherichia coli and obtained rPDIA3 at 97.8% purity using consecutive His-tag and reverse-phase chromatography. Elongated peptide tags screened from artificially designated library had dual functions for protein expression and simple purification.
Keywords
Protein disulfide isomerase A3; elongation mutagenesis;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Park WJ, You SH, Choi HA, Chu YJ, Kim GJ. 2015. Over-expression of recombinant proteins with N-terminal His-tag via subcellular uneven distribution in Escherichia coli. Acta Biochim. Biophys. Sin. (Shanghai) 47: 488-495.   DOI
2 Espah Borujeni A, Channarasappa AS, Salis HM. 2014. Translation rate is controlled by coupled trade-offs between site accessibil- ity, selective RNA unfolding and sliding at upstream standby sites. Nucleic Acids Res. 42: 2646-2659.   DOI
3 Guo F, Wu J, Yang L, Xu G. 2015. Soluble and functional expression of a recombinant enantioselective amidase from Klebsiella oxytoca KCTC 1686 in Escherichia coli and its biochemical characterization. Process Biochem. 50: 1264-1271.   DOI
4 Cheong DE, Ko KC, Han Y, Jeon HG, Sung BH, Kim GJ, et al. 2015. Enhancing functional expression of heterologous proteins through random substitution of genetic codes in the 5' coding region. Biotechnol. Bioeng. 112: 822-826.   DOI
5 Urban-Chmiel R, Dec M, Puchalski A, Wernicki A. 2013. Characterization of heat-shock proteins in Escherichia coli strains under thermal stress in vitro. J. Med. Microbiol. 62: 1897-1901.   DOI
6 Hoffmann F, Rinas U. 2004. Stress induced by recombinant pro- tein production in Escherichia Coli. Advances in Biochemical Engineering/Biotechnology 89: 73-92.
7 Hengen P. 1995. Purification of His-Tag fusion proteins from Escherichia coli. Trends Biochem. Sci. 20: 285-286.   DOI
8 Fischer NO, Blanchette CD, Chromy BA, Kuhn EA, Segelke BW, Corzett M, et al. 2009. Immobilization of His-tagged proteins on nickel-chelating nanolipoprotein particles. Bioconjug. Chem. 20: 460-465.   DOI
9 Freedman RB, Hirst TR, Tuite MF. 1994. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19: 331-336.   DOI
10 Galligan JJ, Petersen DR. 2012. The human protein disulfide isomerase gene family. Hum. Genomics. 6: 6-7364-6-6.   DOI
11 Hatahet F, Ruddock LW. 2009. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal. 11: 2807-2850.   DOI
12 Raykhel I, Alanen H, Salo K, Jurvansuu J, Nguyen VD, Latva-Ranta M, et al. 2007. A molecular specificity code for the three mammalian KDEL receptors. J. Cell Biol. 179: 1193-1204.   DOI
13 Choe MH, Min JW, Jeon HB, Cho DH, Oh JS, Lee HG, et al. 2015. ERp57 modulates STAT3 activity in radioresistant laryngeal cancer cells and serves as a prognostic marker for laryngeal cancer. Oncotarget 6: 2654-2666.
14 Gaucci E, Altieri F, Turano C, Chichiarelli S. 2013. The protein ERp57 contributes to EGF receptor signaling and internalization in MDA-MB-468 breast cancer cells. J. Cell. Biochem. 114: 2461- 2470.   DOI
15 Gonzalez-Perez P, Woehlbier U, Chian RJ, Sapp P, Rouleau GA, Leblond CS, et al. 2015. Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients. Gene 566: 158-165.   DOI
16 Wise R, Duhachek-Muggy S, Qi Y, Zolkiewski M, Zolkiewska A. 2016. Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells. Breast Cancer Res. Treat. 157: 241-252.   DOI
17 Hoffman SM, Chapman DG, Lahue KG, Cahoon JM, Rattu GK, Daphtary N, et al. 2016. Protein disulfide isomerase-endoplasmic reticulum resident protein 57 regulates allergen-induced airways inflammation, fibrosis, and hyperresponsiveness. J. Allergy Clin. Immunol. 137: 822-32.e7.   DOI
18 Altmann C, Hardt S, Fischer C, Heidler J, Lim HY, Haussler A, et al. 2016. Progranulin overexpression in sensory neurons attenuates neuropathic pain in mice: Role of autophagy. Neurobiol. Dis. 96: 294-311.   DOI
19 Torres M, Medinas DB, Matamala JM, Woehlbier U, Cornejo VH, Solda T, et al. 2015. The protein-disulfide Isomerase ERp57 regulates the steady-state levels of the prion protein. J. Biol. Chem. 290: 23631-23645.   DOI
20 Dihazi H, Dihazi GH, Bibi A, Eltoweissy M, Mueller CA, Asif AR, et al. 2013. Secretion of ERP57 is important for extracellular matrix accumulation and progression of renal fibrosis, and is an early sign of disease onset. J. Cell. Sci. 126: 3649-3663.   DOI
21 Nardai G, Stadler K, Papp E, Korcsmaros T, Jakus J, Csermely P. 2005. Diabetic changes in the redox status of the microsomal protein folding machinery. Biochem. Biophys. Res. Commun. 334: 787-795.   DOI
22 Wilding C, Bell K, Funke S, Beck S, Pfeiffer N, Grus FH. 2015. GFAP antibodies show protective effect on oxidatively stressed neuroretinal cells via interaction with ERP57. J. Pharmacol. Sci. 127: 298-304.   DOI
23 Leys CM, Nomura S, LaFleur BJ, Ferrone S, Kaminishi M, Montgomery E, et al. 2007. Expression and prognostic significance of prothymosin-alpha and ERp57 in human gastric cancer. Surgery 141: 41-50.   DOI
24 Doroudi M, Plaisance MC, Boyan BD, Schwartz Z. 2015. Membrane actions of $1{\alpha}$,25(OH)2D3 are mediated by Ca(2+)/calmodulin-dependent protein kinase II in bone and cartilage cells. J. Steroid Biochem. Mol. Biol. 145: 65-74.   DOI
25 Wang Y, Chen J, Lee CS, Nizkorodov A, Riemenschneider K, Martin D, et al. 2010. Disruption of Pdia3 gene results in bone abnormality and affects $1{\alpha}$,25-dihydroxy-vitamin D3-induced rapid activation of PKC. J. Steroid Biochem. Mol. Biol. 121: 257-260.   DOI
26 Yang WS, Yu H, Kim JJ, Lee MJ, Park SK. 2016. Vitamin D-induced ectodomain shedding of TNF receptor 1 as a nongenomic action: D3 vs D2 derivatives. J. Steroid Biochem. Mol. Biol. 155: 18-25.   DOI
27 Stenstrom CM, Holmgren E, Isaksson LA. 2001. Cooperative effects by the initiation codon and its flanking regions on translation initiation. Gene 273: 259-265.   DOI
28 Sepulveda M, Rozas P, Hetz C, Medinas DB. 2016. ERp57 as a novel cellular factor controlling prion protein biosynthesis: Therapeutic potential of protein disulfide isomerases. Prion 10: 50-56.   DOI
29 Choi ES, Han SS, Cheong DE, Park MY, Kim JS, Kim GJ. 2010. Generation of a fast maturating red fluorescent protein by a combined approach of elongation mutagenesis and functional salvage screening. Biochem. Biophys. Res. Commun. 391: 598-603.   DOI
30 Horwich AL, Fenton WA, Chapman E, Farr GW. 2007. Two families of chaperonin: physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23: 115-145.   DOI