Skip to main content
SpringerLink
Log in

Physicochemical Properties of Photoconvertible Fluorescent Protein from Montastraea cavernosa

  • Published:
Russian Journal of Bioorganic Chemistry Aims and scope Submit manuscript

Abstract

Among the wide variety of currently known fluorescent probes, photoconvertible fluorescent proteins (PCFPs), which are capable to irreversibly change their maximum of fluorescence emission under specific light irradiation, are of special interest. In this work, we have studied the basic physicochemical properties of PCFP isolated from Montastraea cavernosa (mcavGR). It has been shown that mcavGR demonstrates both high brightness and photoconversion contrast, which is comparable with the best homologous PCFPs, such as Kaede, dendFP, Dendra2, EosFP, etc., and at the same time has significant photostability.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.

Similar content being viewed by others

REFERENCES

  1. Chudakov, D.M., Matz, M.V., Lukyanov, S., and Lukyanov, K.A., Physiol. Rev. Am. Physiol. Soc., 2010, vol. 90, pp. 1103–1163. https://doi.org/10.1152/physrev.00038.2009

    Article  CAS  Google Scholar 

  2. Martynov, V.I., Pakhomov, A.A., Popova, N.V., Deyev, I.E., and Petrenko, A.G., Acta Naturae, 2016, vol. 8, pp. 33–46.

    Article  CAS  Google Scholar 

  3. Tomosugi, W., Matsuda, T., Tani, T., Nemoto, T., Kotera, I., Saito, K., Horikawa, K., and Nagai, T., Nat. Methods, 2009, vol. 6, pp. 351–353. https://doi.org/10.1038/nmeth.1317

    Article  CAS  PubMed  Google Scholar 

  4. Shinoda, H., Ma, Y., Nakashima, R., Sakurai, K., Matsuda, T., and Nagai, T., Cell Chem. Biol., 2018, pp. 330e7–338e7. https://doi.org/10.1016/j.chembiol.2017.12.005

  5. Pakhomov, A.A. and Martynov, V.I., Biochem. Biophys. Res. Commun., 2011, vol. 407, pp. 230–235. https://doi.org/10.1016/j.bbrc.2011.03.004

    Article  CAS  PubMed  Google Scholar 

  6. Pakhomov, A.A., Frolova, A.Y., Tabakmakher, V.M., Chugunov, A.O., Efremov, R.G., and Martynov, V.I., J. Photochem. Photobiol. B, 2020, vol. 206, p. 111 853. https://doi.org/10.1016/j.jphotobiol.2020.111853

    Article  CAS  Google Scholar 

  7. Fabritius, A., Ng, D., Kist, A.M., Erdogan, M., Portugues, R., and Griesbeck, O., Cell Chem. Biol., 2018, vol. 25, pp. 1554e8–1561e8. https://doi.org/10.1016/j.chembiol.2018.08.008

  8. Kostyuk, A.I., Demidovich, A.D., Kotova, D.A., Belousov, V.V., and Bilan, D.S., Int. J. Mol. Sci., 2019, vol. 20, p. 4200. https://doi.org/10.3390/ijms20174200

    Article  CAS  PubMed Central  Google Scholar 

  9. Martynov, V.I., Pakhomov, A.A., Deyev, I.E., and Petrenko, A.G., Biochim. Biophys. Acta—Gen. Subj., 2018, vol. 1862, pp. 2924–2939.

    Article  CAS  Google Scholar 

  10. Bukhari, H. and Muller, T., Trends Cell Biol., 2019, vol. 29, pp. 912–928. https://doi.org/10.1016/j.tcb.2019.08.004

    Article  CAS  PubMed  Google Scholar 

  11. Mozhaev, A.A., Serova, O.V., Orsa, A.N., Boyko, A.A., Goryashchenko, A.S., Deyev, I.E., and Petrenko, A.G., Russ. J. Bioorg. Chem., 2019, vol. 45, pp. 179–182. https://doi.org/10.1134/S1068162019020080

    Article  CAS  Google Scholar 

  12. Zlobovskaya, O.A., Shirmanova, M.V., Kovaleva, T.F., Sarkisyan, K.S., Zagaynova, E.V., and Lukyanov, K.A., Russ. J. Bioorg. Chem., 2018, vol. 44, pp. 645–652. https://doi.org/10.1134/S1068162018060109

    Article  CAS  Google Scholar 

  13. Adam, V., Histochem. Cell Biol., 2014, vol. 142, pp. 19–41. https://doi.org/10.1007/s00418-014-1190-5

    Article  CAS  PubMed  Google Scholar 

  14. Nemet, I., Ropelewski, P., and Imanishi, Y., Photochem. Photobiol. Sci., 2015, vol. 14, pp. 1787–1806. https://doi.org/10.1039/C5PP00174A

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  15. Ando, R., Hama, H., Yamamoto-Hino, M., Mizuno, H., and Miyawaki, A., Proc. Natl. Acad. Sci. U. S. A., 2002, vol. 99, pp. 12 651–12 656. https://doi.org/10.1073/pnas.202320599

    Article  CAS  Google Scholar 

  16. Fron, E., Sliwa, M., Adam, V., Michiels, J., Rocha, S., Dedecker, P., Hofkens, J., and Mizuno, H., Photochem. Photobiol. Sci., 2014, vol. 13, pp. 867–874. https://doi.org/10.1039/c3pp50335f

    Article  CAS  PubMed  Google Scholar 

  17. Mizuno, H., Mal, T.K., Tong, K.I., Ando, R., Furuta, T., Ikura, M., and Miyawaki, A., Mol. Cell, 2003, vol. 12, pp. 1051–1058. https://doi.org/10.1016/S1097-2765(03)00393-9

    Article  CAS  PubMed  Google Scholar 

  18. Li, X., Chung, L.W., Mizuno, H., Miyawaki, A., and Morokuma, K., J. Phys. Chem. B, vol. 114, pp. 16 666–16 675. https://doi.org/10.1021/jp1101779

  19. Chudakov, D.M., Lukyanov, S., and Lukyanov, K.A., Nat. Protoc., 2007, vol. 2, pp. 2024–2032. https://doi.org/10.1038/nprot.2007.291

    Article  CAS  PubMed  Google Scholar 

  20. Baker, S.M., Buckheit, R.W., and Falk, M.M., BMC Cell Biol., 2010, vol. 11, p. 15. https://doi.org/10.1186/1471-2121-11-15

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  21. Hoi, H., Shaner, N.C., Davidson, M.W., Cairo, C.W., Wang, J., and Campbell, R.E., J. Mol. Biol., 2010, vol. 401, pp. 776–791. https://doi.org/10.1016/j.jmb.2010.06.056

    Article  CAS  PubMed  Google Scholar 

  22. Moeyaert, B., Holt, G., Madangopal, R., Perez-Alvarez, A., Fearey, B.C., Trojanowski, N.F., Ledderose, J., Zolnik, T.A., Das, A., Patel, D., Brown, T.A., Sachdev, R.N.S., Eickholt, B.J., Larkum, M.E., Turrigiano, G.G., Dana, H., Gee, C.E., Oertner, T.G., Hope, B.T., and Schreiter, E.R., Nat. Commun., 2018, vol. 9, p. 4440. https://doi.org/10.1038/s41467-018-06935-2

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Osugi, T., Sasakura, Y., and Satake, H., Sci. Rep., vol. 10, p. 1892. https://doi.org/10.1038/s41598-020-58884-w

  24. Betzig, E., Patterson, G.H., Sougrat, R., Lindwasser, O.W., Olenych, S., Bonifacino, J.S., Davidson, M.W., Lippincott-Schwartz, J., and Hess, H.F., Science, 2006, vol. 313, pp. 1642–1645. https://doi.org/10.1126/science.1127344

    Article  PubMed  Google Scholar 

  25. McKinney, S.A., Murphy, C.S., Hazelwood, K.L., Davidson, M.W., and Looger, L.L., Nat. Methods, 2009, vol. 6, pp. 131–133. https://doi.org/10.1038/nmeth.1296

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  26. Nienhaus, K. and Ulrich Nienhaus, G., Chem. Soc. Rev., 2014, vol. 43, pp. 1088–1106. https://doi.org/10.1039/C3CS60171D

    Article  CAS  PubMed  Google Scholar 

  27. Robert, A., Hookway, C., and Gelfand, V.I., BioEssays, 2016, vol. 38, pp. 232–243. https://doi.org/10.1002/bies.201500142

    Article  PubMed  PubMed Central  Google Scholar 

  28. Habuchi, S., Tsutsui, H., Kochaniak, A.B., Miyawaki, A., and van Oijen, A.M., PLoS One, 2008, vol. 3, pp. 1–9. https://doi.org/10.1371/journal.pone.0003944

    Article  CAS  Google Scholar 

  29. Adam, V., Moeyaert, B., David, C.C., Mizuno, H., Lelimousin, M., Dedecker, P., Ando, R., Miyawaki, A., Michiels, J., Engelborghs, Y., and Hofkens, J., Chem. Biol., 2011, vol. 18, pp. 1241–1251.

    Article  CAS  Google Scholar 

  30. McEvoy, A.L., Hoi, H., Bates, M., Platonova, E., Cranfill, P.J., Baird, M.A., Davidson, M.W., Ewers, H., Liphardt, J., and Campbell, R.E., PLoS One, 2012, vol. 7, e51 314. https://doi.org/10.1371/journal.pone.0051314

    Article  CAS  Google Scholar 

  31. Labas, Y.A., Gurskaya, N.G., Yanushevich, Y.G., Fradkov, A.F., Lukyanov, K.A., Lukyanov, S.A., and Matz, M.V., Proc. Natl. Acad. Sci. U. S. A., 2002, vol. 99, pp. 4256–4261. https://doi.org/10.1073/pnas.062552299

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  32. Wiedenmann, J., Ivanchenko, S., Oswald, F., Schmitt, F., Rocker, C., Salih, A., Spindler, K.-D., and Nienhaus, G.U., Proc. Natl. Acad. Sci. U. S. A., 2004, vol. 101, pp. 15 905–15 910. https://doi.org/10.1073/pnas.0403668101

    Article  CAS  Google Scholar 

  33. Pakhomov, A.A., Martynova, N.Yu., Gurskaya, N.G., Balashova, T.A., and Martynov, V.I., Biochemistry (Moscow), 2004, vol. 69, pp. 901–908. https://doi.org/10.1023/B:BIRY.0000040223.09641.29

    Article  CAS  PubMed  Google Scholar 

  34. Ando, R., Mizuno, H., and Miyawaki, A., Science, 2004, vol. 306, pp. 1370–1373. https://doi.org/10.1126/science.1102506

    Article  CAS  PubMed  Google Scholar 

  35. Karasawa, S., Araki, T., Yamamoto-Hino, M., and Miyawaki, A., J. Biol. Chem., 2003, vol. 278, pp. 34 167–34 171. https://doi.org/10.1074/jbc.M304063200

    Article  CAS  Google Scholar 

  36. Tsutsui, H., Karasawa, S., Shimizu, H., Nukina, N., and Miyawaki, A., EMBO Rep., 2005, vol. 6, pp. 233–238. https://doi.org/10.1038/sj.embor.7400361

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  37. Ai, H.W., Biochem. J., 2006, vol. 400, pp. 531–540.

    Article  CAS  Google Scholar 

  38. Kelmanson, I.V. and Matz, M.V., Mol. Biol. Evol., 2003, vol. 20, pp. 1125–1133. https://doi.org/10.1093/molbev/msg130

    Article  CAS  PubMed  Google Scholar 

  39. Field, S.F., Bulina, M.Y., Kelmanson, I.V., Bielawski, J.P., and Matz, M.V., J. Mol. Evol., 2006, vol. 62, pp. 332–339. https://doi.org/10.1007/s00239-005-0129-9

    Article  CAS  PubMed  Google Scholar 

  40. Kim, H., Grunkemeyer, T.J., Modi, C., Chen, L., Fromme, R., Matz, M.V., and Wachter, R.M., Biochemistry, 2013, vol. 52, pp. 8048–8059. https://doi.org/10.1021/bi401000e

    Article  CAS  PubMed  Google Scholar 

  41. Kim, H., Zou, T., Modi, C., Dorner, K., Grunkemeyer, T.J., Chen, L., Fromme, R., Matz, M.V., Ozkan, S.B., and Wachter, R.M., Structure, 2015, vol. 23, pp. 34–43. https://doi.org/10.1016/j.str.2014.11.011

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  42. Mazel, C.H., Lesser, M.P., Gorbunov, M.Y., Barry, T.M., Farrell, J.H., Wyman, K.D., and Falkowski, P.G., Limnol. Oceanogr., 2003, vol. 48, pp. 402–411. https://doi.org/10.4319/lo.2003.48.1_part_2.0402

    Article  CAS  Google Scholar 

  43. Lambert, T.J., Nat. Methods, 2019, vol. 16, pp. 277–278. https://doi.org/10.1038/s41592-019-0352-8

    Article  CAS  PubMed  Google Scholar 

  44. Pakhomov, A.A., Chertkova, R.V., and Martynov, V.I., Russ. J. Bioorg. Chem., 2015, vol. 41, pp. 602–606. https://doi.org/10.1134/S1068162015060114

    Article  CAS  Google Scholar 

  45. Pletneva, N.V., Pletnev, S., Pakhomov, A.A., Chertkova, R.V., Martynov, V.I., Muslinkina, L., Dauter, Z., and Pletnev, V.Z., Acta Crystallogr. Sect. D Struct. Biol., 2016, vol. 72, pp. 922–932. https://doi.org/10.1107/S205979831601038X

    Article  CAS  Google Scholar 

  46. Tsutsui, H., Shimizu, H., Mizuno, H., Nukina, N., Furuta, T., and Miyawaki, A., Chem. Biol., 2009, vol. 16, pp. 1140–1147. https://doi.org/10.1016/j.chembiol.2009.10.010

    Article  CAS  PubMed  Google Scholar 

  47. Paez-Segala, M.G., Sun, M.G., Shtengel, G., Viswanathan, S., Baird, M.A., Macklin, J.J., Patel, R., Allen, J.R., Howe, E.S., Piszczek, G., Hess, H.F., Davidson, M.W., Wang, Y., and Looger, L.L., Nat. Methods, 2015, vol. 12, pp. 215–218. https://doi.org/10.1038/nmeth.3225

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  48. Pakhomov, A.A., Martynov, V.I., Orsa, A.N., Bondarenko, A.A., Chertkova, R.V., Lukyanov, K.A., Petrenko, A.G., and Deyev, I.E., Biochem. Biophys. Res. Commun., 2017, vol. 493, pp. 1518–1521. https://doi.org/10.1016/j.bbrc.2017.09.170

    Article  CAS  PubMed  Google Scholar 

  49. Katoh, K. and Toh, H., Bioinformatics, 2007, vol. 23, pp. 372–374. https://doi.org/10.1093/bioinformatics/btl592

    Article  CAS  PubMed  Google Scholar 

  50. Gouy, M., Guindon, S., and Gascuel, O., Mol. Biol. Evol., 2010, vol. 27, pp. 221–224. https://doi.org/10.1093/molbev/msp259

    Article  CAS  PubMed  Google Scholar 

  51. Guindon, S., Dufayard, J.-F., Lefort, V., Anisimova, M., Hordijk, W., and Gascuel, O., Syst. Biol., 2010, vol. 59, pp. 307–321. https://doi.org/10.1093/sysbio/syq010

    Article  CAS  PubMed  Google Scholar 

  52. Orm, M., Cubitt, A.B., Kallio, K., Gross, L.A., Tsien, R.Y., and Remington, S.J., Science, 1996, vol. 273, pp. 1392–1395. https://doi.org/10.1126/science.273.5280.139

    Article  Google Scholar 

  53. Baird, G.S., Zacharias, D.A., and Tsien, R.Y., Proc. Natl. Acad. Sci. U. S. A., 2000, vol. 97, pp. 11 984–11 989. https://doi.org/10.1073/pnas.97.22.11984

    Article  Google Scholar 

  54. Ward, W.W., Green Fluorescent Protein: Properties, Applications, and Protocols, 2nd ed., Chalfie, M. and Kain, S.R., Eds., Wiley, 2005, pp. 39–65. https://doi.org/10.1002/0471739499.ch3

    Book  Google Scholar 

  55. Sniegowski, J.A., Phail, M.E., and Wachter, R.M., Biochem. Biophys. Res. Commun., 2005, vol. 332, pp. 657–663. https://doi.org/10.1016/j.bbrc.2005.04.166

    Article  CAS  PubMed  Google Scholar 

  56. Hoops, S., Sahle, S., Gauges, R., Lee, C., Pahle, J., Simus, N., Singhal, M., Xu, L., Mendes, P., and Kummer, U., Bioinformatics, 2006, vol. 22, pp. 3067–3074. https://doi.org/10.1093/bioinformatics/btl485

    Article  CAS  PubMed  Google Scholar 

Download references

ACKNOWLEDGMENTS

The authors thank K.A. Lukyanov from the Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences for providing plasmids that carried the gene of the mcavGR fluorescent protein.

Funding

The work was supported by grants nos. 18-04-00745 and 18-29-09166 from the Russian Foundation for Basic Research and, partially, grant no. 19-73-20194 from Russian Science Foundation.

Author information

Authors and Affiliations

  1. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia

    A. Yu. Frolova, A. A. Pakhomov & V. I. Martynov

  2. Nesmeyanov Institute of Organoelement Compounds, 119334, Moscow, Russia

    A. Yu. Frolova & A. A. Pakhomov

Authors
  1. A. Yu. Frolova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. A. A. Pakhomov
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. V. I. Martynov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to A. A. Pakhomov.

Ethics declarations

COMPLIANCE WITH ETHICAL STANDARDS

This article does not contain any studies with the use of humans as objects of research.

Conflict of Interests

The authors state that there is no conflict of interest.

Additional information

Translated by A. Levina

Abbreviations: FP, fluorescent protein; PCFP, Photoconvertible Fluorescent Protein; dendFP, PCFP from Dendronephthya sp.; Dendra2, monomeric mutant variant of dendFP; Kaede, PCFP from Trachyphyllia geoffroyi; mcavGR, mcavRFP, PCFP from Montastraea cavernosa.

Corresponding author: phone: +7 (495) 336-51-11; fax: +7 (495) 336-61-66.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Frolova, A.Y., Pakhomov, A.A. & Martynov, V.I. Physicochemical Properties of Photoconvertible Fluorescent Protein from Montastraea cavernosa . Russ J Bioorg Chem 47, 244–251 (2021). https://doi.org/10.1134/S1068162021010052

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1068162021010052

Keywords

Search

Navigation