GFP fusion promotes the soluble and active expression of a pea actin isoform (PEAc1) in Escherichia coli

References

• Wasteneys, G. O.; Galway, M. E. Remodeling the Cytoskeleton for Growth and Form: An Overview with Some New Views. Annu. Rev. Plant Biol. 2003, 54, 691–722. DOI: 10.1146/annurev.arplant.54.031902.134818.
   PubMed Web of Science ®Google Scholar
• Meagher, R. B. Divergence and Differential Expression of Actin Gene Families in Higher Plants. In International Review of Cytology, Jeon, K. W., Friedlander, M., Eds.; Academic Press: New York, 1991; Vol. 125, pp. 139–163.
   Google Scholar
• Kandasamy, M. K.; McKinney, E. C.; Meagher, R. B. Functional Nonequivalency of Actin Isovariants inArabidopsis. Mol. Biol. Cell 2002, 13, 251–261. DOI: 10.1091/mbc.01-07-0342.
   PubMed Web of Science ®Google Scholar
• Hu, S.; Yen, L. Sequence Analysis of Pea Tendril Actin Isoform II cDNA Clones. Chinese J. Biochem. Mol. Biol. 1999, 15, 857–860.
   Google Scholar
• Huang, S.; Liu, J.; Yan, L.; Peng, X. Developmental-Stage and Organ-Specific Expression of Actin Genes in Seedlings of Pisum satium. J. China Agr. Univ. 1997, 2, 25–29.
   Google Scholar
• Xiaofeng, C.; Rongchen, W.; Yan, L.; Zhibin, L.; Naisui, P.; Zhangliang, C. Construction of a Pea Tendril cDNA Library and Sequence Analysis of a Pea Actin cDNA, PEAc l. Chinese Sci. Bull. 1994, 39, 332–337.
   Google Scholar
• Yi, L.; Wuling, Z. Specific Expression of Pea Isoactin Genes. Chinese Bull. Bot. 2001, 18, 76–80.
   Google Scholar
• Parveen, S.; Rahman, A. Actin Isovariant ACT7 Modulates Root Thermomorphogenesis by Altering Intracellular Auxin Homeostasis. IJMS 2021, 22, 7749. DOI: 10.3390/ijms22147749.
   Google Scholar
• Gilliland, L. U.; Pawloski, L. C.; Kandasamy, M. K.; Meagher, R. B. Arabidopsis Actin Gene ACT7 Plays an Essential Role in Germination and Root Growth. Plant J. 2003, 33, 319–328. DOI: 10.1046/j.1365-313x.2003.01626.x.
   PubMed Web of Science ®Google Scholar
• McDowell, J. M.; An, Y. Q.; Huang, S.; McKinney, E. C.; Meagher, R. B. The Arabidopsis ACT7 Actin Gene is Expressed in Rapidly Developing Tissues and Responds to Several External Stimuli. Plant Physiol. 1996, 111, 699–711. DOI: 10.1104/pp.111.3.699.
   PubMed Web of Science ®Google Scholar
• Liu, X.; Yen, L. F. Purification and Characterization of Actin from Maize Pollen 1. Plant Physiol. 1992, 99, 1151–1155. DOI: 10.1104/pp.99.3.1151.
   PubMed Web of Science ®Google Scholar
• Ren, H.; Gibbon, B. C.; Ashworth, S. L.; Sherman, D. M.; Yuan, M.; Staiger, C. J. Actin Purified from Maize Pollen Functions in Living Plant Cells. Plant Cell 1997, 9, 1445–1457. DOI: 10.2307/3870394.
   PubMed Web of Science ®Google Scholar
• DÍAz-Camino, C.; Villanueva, M. A. Purification of Multiple Functional Leaf-Actin Isoforms from Phaseolus vulgaris L. Biochem J. 1999, 343, 597–602. DOI: 10.1042/0264-6021:3430597.
   PubMed Web of Science ®Google Scholar
• Kijima, S. T.; Staiger, C. J.; Katoh, K.; Nagasaki, A.; Ito, K.; Uyeda, T. Q. P. Arabidopsis Vegetative Actin Isoforms, AtACT2 and AtACT7, Generate Distinct Filament Arrays in Living Plant Cells. Sci. Rep. 2018, 8, 4381. DOI: 10.1038/s41598-018-22707-w.
   PubMed Web of Science ®Google Scholar
• Xiong, R.; Chen, Z.; Wang, W.; Jiang, L.; Xiang, Y.; Fan, J. Combined Transcriptome Sequencing and Prokaryotic Expression to Investigate the Key Enzyme in the 2-C-Methylerythritol-4-Phosphate Pathway of Osmanthus fragrans. Funct. Plant Biol. 2020, 47, 945–958. DOI: 10.1071/FP19365.
   PubMed Web of Science ®Google Scholar
• Ki, M.-R.; Pack, S. P. Fusion Tags to Enhance Heterologous Protein Expression. Appl. Microbiol. Biotechnol. 2020, 104, 2411–2425. DOI: 10.1007/s00253-020-10402-8.
   PubMed Web of Science ®Google Scholar
• Liu, A. X.; Zhang, S. B.; Xu, X. J.; Ren, D. T.; Liu, G. Q. Soluble Expression and Characterization of a GFP-Fused Pea Actin Isoform (PEAc1). Cell Res. 2004, 14, 407–414. DOI: 10.1038/sj.cr.7290241.
   PubMed Web of Science ®Google Scholar
• Tsien, R. Y. The Green Fluorescent Protein. Annu. Rev. Biochem. 1998, 67, 509–544. DOI: 10.1146/annurev.biochem.67.1.509.
   PubMed Web of Science ®Google Scholar
• Timmers, A. C. J.; Niebel, A.; Balagué, C.; Dagkesamanskaya, A. Differential Localisation of GFP Fusions to Cytoskeleton-Binding Proteins in Animal, Plant, and Yeast Cells. Protoplasma 2002, 220, 69–0078. DOI: 10.1007/s00709-002-0026-7.
   PubMed Web of Science ®Google Scholar
• Ma, Z.; Sun, Y.; Zhu, X.; Yang, L.; Chen, X.; Miao, Y. Membrane Nanodomains Modulate Formin Condensation for Actin Remodeling in Arabidopsis Innate Immune Responses. Plant Cell 2022, 34, 374–394. DOI: 10.1093/plcell/koab261.
   PubMed Web of Science ®Google Scholar
• Waldo, G. S.; Standish, B. M.; Berendzen, J.; Terwilliger, T. C. Rapid Protein-Folding Assay Using Green Fluorescent Protein. Nat. Biotechnol. 1999, 17, 691–695. DOI: 10.1038/10904.
   PubMed Web of Science ®Google Scholar
• Bakholdina, S. I.; Stenkova, A. M.; Bystritskaya, E. P.; Sidorin, E. V.; Kim, N. Y.; Menchinskaya, E. S.; Gorpenchenko, T. Y.; Aminin, D. L.; Shved, N. A.; Solov’eva, T. F. Studies on the Structure and Properties of Membrane Phospholipase A1 Inclusion Bodies Formed at Low Growth Temperatures Using GFP Fusion Strategy. Molecules 2021, 26, 3936. DOI: 10.3390/molecules26133936.
   PubMed Web of Science ®Google Scholar
• Bernhofer, M.; Dallago, C.; Karl, T.; Satagopam, V.; Heinzinger, M.; Littmann, M.; Olenyi, T.; Qiu, J.; Schütze, K.; Yachdav, G.; et al. PredictProtein - Predicting Protein Structure and Function for 29 Years. Nucleic Acids Res. 2021, 49, W535–W540. DOI: 10.1093/nar/gkab354.
   PubMed Web of Science ®Google Scholar
• PredictProtein. Available online: https://predictprotein.org.
   Google Scholar
• Fox, J. E. B.; Dockter, M. E.; Phillips, D. R. An Improved Method for Determining the Actin Filament Content of Nonmuscle Cells by the DNase I Inhibition Assay. Anal. Biochem. 1981, 117, 170–177. DOI: 10.1016/0003-2697(81)90707-7.
   PubMed Web of Science ®Google Scholar
• Hager, D. A.; Burgess, R. R. Elution of Proteins from Sodium Dodecyl Sulfate-Polyacrylamide Gels, Removal of Sodium Dodecyl Sulfate, and Renaturation of Enzymatic Activity: Results with Sigma Subunit of Escherichia coli RNA Polymerase, Wheat Germ DNA Topoisomerase, and Other Enzymes. Anal. Biochem. 1980, 109, 76–86. DOI: 10.1016/0003-2697(80)90013-5.
   PubMed Web of Science ®Google Scholar
• Shaevitz, J. W.; Gitai, Z. The Structure and Function of Bacterial Actin Homologs. Cold Spring Harb. Perspect. Biol. 2010, 2, a000364. DOI: 10.1101/cshperspect.a000364.
   PubMed Web of Science ®Google Scholar
• Agustriana, E.; Nuryana, I.; Laksmi, F. A.; Dewi, K. S.; Wijaya, H.; Rahmani, N.; Yudiargo, D. R.; Ismadara, A.; Hadi, M. I.; Purnawan, A.; et al. Optimized Expression of Large Fragment DNA Polymerase I from Geobacillus stearothermophilus in Escherichia coli Expression System. Prep. Biochem. Biotech. 2022, 1–10. DOI: 10.1080/10826068.2022.2095573.
   PubMed Web of Science ®Google Scholar
• Kim, S. H.; Jeong, H. J. Soluble Expression of Small Antibody Fragments against PD-L1 Using Escherichia coli with High Yield and Purity. Appl. Sci. 2021, 11, 9149. DOI: 10.3390/app11199149.
   Google Scholar
• Bhatwa, A.; Wang, W.; Hassan, Y. I.; Abraham, N.; Li, X. Z.; Zhou, T. Challenges Associated with the Formation of Recombinant Protein Inclusion Bodies in Escherichia coli and Strategies to Address Them for Industrial Applications. Front. Bioeng. Biotechnol. 2021, 9, 630551. DOI: 10.3389/fbioe.2021.630551.
   PubMed Web of Science ®Google Scholar
• Rücker, E.; Schneider, G.; Steinhäuser, K.; Löwer, R.; Hauber, J.; Stauber, R. H. Rapid Evaluation and Optimization of Recombinant Protein Production Using GFP Tagging. Protein Expr. Purif. 2001, 21, 220–223. DOI: 10.1006/prep.2000.1373.
   PubMed Web of Science ®Google Scholar
• Buzan, J.; Du, J.; Karpova, T.; Frieden, C. Histidine-Tagged Wild-Type Yeast Actin: Its Properties and Use in an Approach for Obtaining Yeast Actin Mutants. Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 2823–2827. DOI: 10.1073/pnas.96.6.2823.
   PubMed Web of Science ®Google Scholar
• Verkhusha, V. V.; Shavlovsky, M. M.; Nevzglyadova, O. V.; Gaivoronsky, A. A.; Artemov, A. V.; Stepanenko, O. V.; Kuznetsova, I. M.; Turoverov, K. K. Expression of Recombinant GFP-Actin Fusion Protein in the Methylotrophic Yeast Pichia pastoris. FEMS Yeast Res. 2003, 3, 105–111. DOI: 10.1016/S1567-1356(02)00160-5.
   PubMed Web of Science ®Google Scholar
• Kuznetsova, I. M.; Biktashev, A. G.; Khaitlina, S. Y.; Vassilenko, K. S.; Turoverov, K. K.; Uversky, V. N. Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin. Biophys. J. 1999, 77, 2788–2800. DOI: 10.1016/S0006-3495(99)77111-0.
   PubMed Web of Science ®Google Scholar
• Zhang, T. Connecting the Dots: Membrane Nanodomains Mediate Clustering of Actin-Nucleator Type I Formins in Arabidopsis Immune Responses. Plant Cell 2022, 34, 6–7. DOI: 10.1093/plcell/koab277.
   PubMed Web of Science ®Google Scholar
• Kabsch, W.; Mannherz, H. G.; Suck, D.; Pai, E. F.; Holmes, K. C. Atomic Structure of the Actin: DNase I Complex. Nature 1990, 347, 37–44. DOI: 10.1038/347037a0.
   PubMed Web of Science ®Google Scholar
• Holmes, K. C.; Popp, D.; Gebhard, W.; Kabsch, W. Atomic Model of the Actin Filament. Nature 1990, 347, 44–49. DOI: 10.1038/347044a0.
   PubMed Web of Science ®Google Scholar
• Dominguez, R.; Holmes, K. C. Actin Structure and Function. Annu. Rev. Biophys. 2011, 40, 169–186. DOI: 10.1146/annurev-biophys-042910-155359.
   PubMed Web of Science ®Google Scholar
• Bubb, M. R.; Senderowicz, A. M.; Sausville, E. A.; Duncan, K. L.; Korn, E. D. Jasplakinolide, a Cytotoxic Natural Product, Induces Actin Polymerization and Competitively Inhibits the Binding of Phalloidin to F-Actin. J. Biol. Chem. 1994, 269, 14869–14871. DOI: 10.1016/S0021-9258(17)36545-6.
   PubMed Web of Science ®Google Scholar
• Welch, M. D.; Mullins, R. D. Cellular Control of Actin Nucleation. Annu. Rev. Cell Dev. Biol. 2002, 18, 247–288. DOI: 10.1146/annurev.cellbio.18.040202.112133.
   PubMed Web of Science ®Google Scholar
• Andersland, J. M.; Jagendorf, A. T.; Parthasarathy, M. V. The Isolation of Actin from Pea Roots by DNase I Affinity Chromatography. Plant Physiol. 1992, 100, 1716–1723. DOI: 10.1104/pp.100.4.1716.
   PubMed Web of Science ®Google Scholar
• Igarashi, H.; Vidali, L.; Yokota, E.; Sonobe, S.; Hepler, P. K.; Shimmen, T. Actin Filaments Purified from Tobacco Cultured by-2 Cells Can Be Translocated by Plant Myosin. Plant Cell Physiol. 1999, 40, 1167–1171. DOI: 10.1093/oxfordjournals.pcp.a029502.
   Web of Science ®Google Scholar
• Mannherz, H. G.; Goody, R. S.; Konrad, M.; Nowak, E. The Interaction of Bovine Pancreatic Deoxyribonuclease I and Skeletal Muscle Actin. Eur. J. Biochem. 1980, 104, 367–379. DOI: 10.1111/j.1432-1033.1980.tb04437.x.
   PubMedGoogle Scholar
• Suck, D.; Lahm, A.; Oefner, C. Structure Refined to 2Å of a Nicked DNA Octanucleotide Complex with DNase I. Nature 1988, 332, 464–468. DOI: 10.1038/332464a0.
   PubMed Web of Science ®Google Scholar
• Boyer, M.; Roustan, C.; Benyamin, Y. DNAse I – Actin Complex: An Immunological Study. Biosci. Rep. 1985, 5, 39–46. DOI: 10.1007/BF01117439.
   PubMed Web of Science ®Google Scholar