About this Journal Submit a Manuscript Table of Contents
Journal of Nanomaterials
Volume 2013 (2013), Article ID 468105, 9 pages
http://dx.doi.org/10.1155/2013/468105
Research Article

A Novel Complex: A Quantum Dot Conjugated to an Active T7 RNA Polymerase

1Niels Bohr Institute, University of Copenhagen, 2100 Copenhagen, Denmark
2Institute of Biology, Eötvös Loránd University, Budapest 1053, Hungary
3Institute of Biology, University of Copenhagen, 2200 Copenhagen, Denmark

Received 28 January 2013; Accepted 17 April 2013

Academic Editor: Christophe Merlin

Copyright © 2013 Mette Eriksen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. J. Stahl and K. Zinn, “Nucleotide sequence of the cloned gene for bacteriophage T7 RNA polymerase,” Journal of Molecular Biology, vol. 148, no. 4, pp. 481–485, 1981. View at Scopus
  2. J. E. Brown, J. F. Klement, and W. T. McAllister, “Sequences of three promoters for the bacteriophage SP6 RNA polymerase,” Nucleic Acids Research, vol. 14, pp. 3521–3526, 1986.
  3. S. Brakmann and S. Grzeszik, “An error-prone T7 RNA polymerase mutant generated by directed evolution,” ChemBioChem, vol. 2, no. 3, pp. 212–219, 2001. View at Scopus
  4. F. W. Studier and B. A. Moffatt, “Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes,” Journal of Molecular Biology, vol. 189, no. 1, pp. 113–130, 1986. View at Scopus
  5. K. Terpe, “Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems,” Applied Microbiology and Biotechnology, vol. 72, no. 2, pp. 211–222, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. M. B. Iskakova, W. Szaflarski, M. Dreyfus, J. Remme, and K. H. Nierhaus, “Troubleshooting coupled in vitro transcription-translation system derived from Escherichia coli cells: synthesis of high-yield fully active proteins,” Nucleic Acids Research, vol. 34, no. 19, article no. e135, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. D. J. Lockhart, H. Dong, M. C. Byrne et al., “Expression monitoring by hybridization to high-density oligonucleotide arrays,” Nature Biotechnology, vol. 14, no. 13, pp. 1675–1680, 1996. View at Scopus
  8. A. R. Krainer, T. Maniatis, B. Ruskin, and M. R. Green, “Normal and mutant human β-globin pre-mRNAs are faithfully and efficiently spliced in vitro,” Cell, vol. 36, no. 4, pp. 993–1005, 1984. View at Scopus
  9. K. Zinn, D. DiMaio, and T. Maniatis, “Identification of two distinct regulatory regions adjacent to the human β-interferon gene,” Cell, vol. 34, no. 3, pp. 865–879, 1983. View at Scopus
  10. S. Wagner, M. M. Klepsch, S. Schlegel et al., “Tuning Escherichia coli for membrane protein overexpression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 38, pp. 14371–14376, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. W. C. W. Chan and S. Nie, “Quantum dot bioconjugates for ultrasensitive nonisotopic detection,” Science, vol. 281, no. 5385, pp. 2016–2018, 1998. View at Publisher · View at Google Scholar · View at Scopus
  12. X. Michalet, F. Pinaud, T. D. Lacoste et al., “Properties of fluorescent semiconductor nanocrystals and their application to biological labeling,” Single Molecules, vol. 2, no. 4, pp. 261–276, 2001.
  13. X. Michalet, F. F. Pinaud, L. A. Bentolila et al., “Quantum dots for live cells, in vivo imaging, and diagnostics,” Science, vol. 307, no. 5709, pp. 538–544, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. D. R. Larson, W. R. Zipfel, R. M. Williams et al., “Water-soluble quantum dots for multiphoton fluorescence imaging in vivo,” Science, vol. 300, no. 5624, pp. 1434–1436, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. M. Dahan, S. Lévi, C. Luccardini, P. Rostaing, B. Riveau, and A. Triller, “Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking,” Science, vol. 302, no. 5644, pp. 442–445, 2003. View at Publisher · View at Google Scholar · View at Scopus
  16. R. Edgar, A. Rokney, M. Feeney et al., “Bacteriophage infection is targeted to cellular poles,” Molecular Microbiology, vol. 68, no. 5, pp. 1107–1116, 2008.
  17. A. Biebricher, W. Wende, C. Escudé, A. Pingoud, and P. Desbiolles, “Tracking of single quantum dot labeled EcoRV sliding along DNA manipulated by double optical tweezers,” Biophysical Journal, vol. 96, no. 8, pp. L50–L52, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. Y. Ebenstein, N. Gassman, S. Kim et al., “Lighting up individual DNA binding proteins with quantum dots,” Nano Letters, vol. 9, no. 4, pp. 1598–1603, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. L. Jauffred, A. C. Richardson, and L. B. Oddershede, “Three-Dimensional optical control of individual quantum dots,” Nano Letters, vol. 8, no. 10, pp. 3376–3380, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. L. Jauffred and L. B. Oddershede, “Two-photon quantum dot excitation during optical trapping,” Nano Letters, vol. 10, no. 5, pp. 1927–1930, 2010.
  21. S. Marín, S. Pujals, E. Giralt, and A. Merkoçi, “Electrochemical investigation of cellular uptake of quantum dots decorated with a proline-rich cell penetrating peptide,” Bioconjugate Chemistry, vol. 22, no. 2, pp. 180–185, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. I. J. Finkelstein, M. L. Visnapuu, and E. C. Greene, “Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase,” Nature, vol. 468, no. 7326, pp. 983–987, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. R. T. Pomerantz, R. Ramjit, Z. Gueroui et al., “A tightly regulated molecular motor based upon T7 RNA polymerase,” Nano Letters, vol. 5, no. 9, pp. 1698–1703, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. B. He, M. Rong, D. Lyakhov et al., “Rapid mutagenesis and purification of phage RNA polymerases,” Protein Expression and Purification, vol. 9, no. 1, pp. 142–151, 1997. View at Publisher · View at Google Scholar · View at Scopus
  25. D. Beckett, E. Kovaleva, and P. J. Schatz, “A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation,” Protein Science, vol. 8, no. 4, pp. 921–929, 1999. View at Scopus
  26. E. Gasteiger, C. Hoogland, A. Gattiker et al., The Proteomics Protocols Handbook: Protein Identification and Analysis Tools on the ExPASy Server, Humana Press, 2003.
  27. J. Tholstrup, L. B. Oddershede, and M. A. Sørensen, “mRNA pseudoknot structures can act as ribosomal roadblocks,” Nucleic Acids Research, vol. 40, pp. 303–313, 2012.
  28. D. Sage, F. R. Neumann, F. Hediger, S. M. Gasser, and M. Unser, “Automatic tracking of individual fluorescence particles: application to the study of chromosome dynamics,” IEEE Transactions on Image Processing, vol. 14, no. 9, pp. 1372–1383, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. R. Edgar, M. McKinstry, J. Hwang et al., “High-sensitivity bacterial detection using biotin-tagged phage and quantum-dot nanocomplexes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 13, pp. 4841–4845, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. W. Bücking, S. Massadeh, A. Merkulov, S. Xu, and T. Nann, “Electrophoretic properties of BSA-coated quantum dots,” Analytical and Bioanalytical Chemistry, vol. 396, no. 3, pp. 1087–1094, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. S. J. Clarke, C. A. Hollmann, F. A. Aldaye, and J. L. Nadeau, “Effect of ligand density on the spectral, physical, and biological characteristics of CdSe/ZnS quantum dots,” Bioconjugate Chemistry, vol. 19, no. 2, pp. 562–568, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. R. Mittal and M. P. Bruchez, “Biotin-4-fluorescein based fluorescence quenching assay for determination of biotin binding capacity of streptavidin conjugated quantum dots,” Bioconjugate Chemistry, vol. 22, no. 3, pp. 362–368, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. H. Zhang, X. Zeng, Q. Li, M. Gaillard-Kelly, C. R. Wagner, and D. Yee, “Fluorescent tumour imaging of type I IGF receptor in vivo: comparison of antibody-conjugated quantum dots and small-molecule fluorophore,” British Journal of Cancer, vol. 101, no. 1, pp. 71–79, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. C. M. Niemeyer, M. Adler, B. Pignataro et al., “Self-assembly of DNA-streptavidin nanostructures and their use as reagents in immuno-PCR,” Nucleic Acids Research, vol. 27, no. 23, pp. 4553–4561, 1999. View at Scopus
  35. J. Richter, M. Adler, and C. M. Niemeyer, “Monte Carlo simulation of the assembly of bis-biotinylated DNA and streptavidin,” ChemPhysChem, vol. 4, no. 1, pp. 79–83, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. L. Jauffred, M. Sletmoen, F. Czerwinski, and L. B. Oddershede, “Quantum dots as handles for optical manipulation,” in Optical Trapping and Optical Micromanipulation VII, vol. 7762 of SPIE Proceedings, 2010.
  37. P. Thomen, P. J. Lopez, U. Bockelmann, J. Guillerez, M. Dreyfus, and F. Heslot, “T7 RNA polymerase studied by force measurements varying cofactor concentration,” Biophysical Journal, vol. 95, no. 5, pp. 2423–2433, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. J. H. Kim and R. G. Larson, “Single-molecule analysis of 1D diffusion and transcription elongation of T7 RNA polymerase along individual stretched DNA molecules,” Nucleic Acids Research, vol. 35, no. 11, pp. 3848–3858, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. G. M. Skinner, C. G. Baumann, D. M. Quinn, J. E. Molloy, and J. G. Hoggett, “Promoter binding, initiation, and elongation by bacteriophage T7 RNA polymerase: a single-molecule view of the transcription cycle,” Journal of Biological Chemistry, vol. 279, no. 5, pp. 3239–3244, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. G. M. Skinner, B. S. Kalafut, and K. Visscher, “Downstream DNA tension regulates the stability of the T7 RNA polymerase initiation complex,” Biophysical Journal, vol. 100, no. 4, pp. 1034–1041, 2011. View at Publisher · View at Google Scholar · View at Scopus