Skip to main content

Different Structural Behaviors Evidenced in Thaumatin-Like Proteins: A Spectroscopic Study

The Protein Journal volume 27, pages 13–20 (2008)Cite this article

Abstract

Three proteins belonging to the thaumatin-like proteins family were compared in this study from a structural point of view: zeamatin, a new recently isolated PR-5 from Cassia didymobotrya and the commercial sweet-thaumatin. The former two proteins possess antifungal activities while commercial thaumatin is well known to be a natural sweetener. Intrinsic fluorescence studies have evidenced that the three proteins behave differently in unfolding experiments showing different structural rigidity. All the three proteins are more stable at slight acidic buffers, but sweet-thaumatin has a major tendency to destructurate itself. Similar observations were made from circular dichroism studies where a structural dependence relationship from the pH and the solvent used confirmed a hierarchic scale of stability for the three proteins. These structural differences should be considered to be significant for a functional role.

This is a preview of subscription content, access via your institution.

Access options

Buy single article

Instant access to the full article PDF.

43,34 €

Price includes VAT (Finland)
Tax calculation will be finalised during checkout.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Abbreviations

PRP:

Pathogenesis related protein

TLPs:

Thaumatin-like proteins

Gdn/HCl:

Guanidine hydrochloride

CHES:

Cyclohexylaminoethanesulfonic acid

Tris:

Tris (hydroxymethyl)aminomethane

Bis-Tris:

Bis (2-hydroxyethyl)imino-tris(hydroxymethyl)aminomethane

CD:

Circular dichroism

TFE:

2,2,2,-Trifluoroethanol

MWR, θ:

Molar mean residue ellipticity

CdTLP:

Cassia didymobotrya Thaumatin-like protein

ATR/FT-IR:

Attenuated Total Reflectance—Fourier Transform Infra Red

MALDI-ToF:

Matrix-assisted laser desorption ionization-time of flight

SDS–PAGE:

Sodium dodecylsulfate–polyacrilamide gel electrophoresis

Trp:

Triptophane

Phe:

Phenylalanine

Tyr:

Tyrosine

References

  1. Selitrennikoff CP (2001) Appl Environ Microbiol 67:2883–2884

    Article  CAS  Google Scholar 

  2. Van Loon LC (1997) Eur J Plant Pathol 103:753–765

    Article  Google Scholar 

  3. Van der Wel H, Loewe K (1972) Eur J Biochem 31:221–2255

    Article  Google Scholar 

  4. De Vos AM, Hatada M, van der Wel H, Krabbendam H, Peerdeman AF, Kim SH (1985) Proc Natl Acad Sci USA 82:1406–1409

    Article  Google Scholar 

  5. Ogata CM, Gordon PF, de Vos AM, Kim SH (1992) J Mol Biol 228:893–908

    Article  CAS  Google Scholar 

  6. Batalia MA, Monzingo AF, Ernst S, Roberts W, Robertus JD (1996) Nat Struct Biol 3:19–23

    Article  CAS  Google Scholar 

  7. Min K, Ha SC, Hasegawa PM, Bressan RA, Yun DJ, Kim KK (2004) Proteins 54:170–173

    Article  CAS  Google Scholar 

  8. Leone P, Menu-Bouaouiche L, Peumans WJ, Payan F, Barre A, Roussel A, Van Damme EJ, Rouge P (2006) Biochimie 88:45–52

    Article  CAS  Google Scholar 

  9. Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F (1997) Plant Cell Physiol 38:783–791

    CAS  Google Scholar 

  10. Barre A, Peumans WJ, Menu-Bouaouiche L, Van Damme EJM, May GD, Herrera AF, Leuven FV, Rouge P (2000) Planta 211:791–799

    Article  CAS  Google Scholar 

  11. Abad LR, D’Urzo MP, Dong L, Narasimhan ML, Reuveni M, Jian KZ (1996) Plant Sci 118:11–23

    Article  CAS  Google Scholar 

  12. Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F (1999) J Mol Biol 286:1137–1145

    Article  CAS  Google Scholar 

  13. Vitali A, Pacini L, Bordi E, De Mori P, Pucillo L, Maras B, Botta B, Brancaccio A, Giardina B (2006) Plant Physiol Biochem 44:604–610

    Article  CAS  Google Scholar 

  14. Roberts WK, Selitrennikoff CP (1990) J Gen Microbiol 136:1771–1778

    CAS  Google Scholar 

  15. Lakowicz JR (1987) Principles of fluorescence spectroscopy. Plenum Press, New York and London

    Google Scholar 

  16. Eftink MR, Shastry MC (1997) Method Enzymol 278:221–257

    CAS  Article  Google Scholar 

  17. Di Stasio E, Bizzarri P, Misiti F, Pavoni E, Brancaccio A (2004) Biophys Chem 107:197–211

    Article  CAS  Google Scholar 

  18. Eftink MR (1994). Biophys J 66:482–501

    CAS  Article  Google Scholar 

  19. Pace CN (1986) Methods Enzymol 131:266–280

    CAS  Google Scholar 

  20. Schellman JA (1987) Annu Rev Biophys Biophys Chem 16:115–137

    Article  CAS  Google Scholar 

  21. Eftink MR (1998) Biochem (Mosc.) 63:276–284

    CAS  Google Scholar 

  22. Wilson S, Mahiou B, Reiger R, Tentler S, Schimoler R, Orndorff S, Selitrennikoff CP (2000) Biotechnol Prog 16:38–43

    Article  CAS  Google Scholar 

  23. Fuchs HC, Bohle B, Dall’Antonia Y, Radauer C, Hoffmann-Sommergruber K, Mari A, Scheiner O, Keller W, Breiteneder H (2006) Clin Exp Allergy 36:359–368

    Article  CAS  Google Scholar 

  24. Byler D.M., Susi H (1986) Biopolymers 25:469–487

    Article  CAS  Google Scholar 

  25. Dong A, Huang P, Caughey WS (1990) Biochemistry 29:3303–3308

    Article  CAS  Google Scholar 

  26. Trudel J, Grenier J, Potvin C, Asselin A (1998) Plant Physiol 118:1431–1438

    Article  CAS  Google Scholar 

  27. Grenier J, Potvin C, Trudel J, Asselin A (1999) Plant J 19:473–80

    Article  CAS  Google Scholar 

  28. Osmond RI, Hrmova M, Fontaine F, Imberty A, Fincher GB (2001) Eur J Biochem 268:4190–4199

    Article  CAS  Google Scholar 

  29. Menu-Bouaouiche L, Vriet C, Peumans JW, Van Damme JM, Rougè P (2003) Biochimie 85:123–131

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was partially supported by grants from Fondi d’Ateneo, Progetto D1 2006, Chatholic University, Rome, Italy. The M.I.U.R. financial support of FIRB 2003 (no. RBNE034XSW) is also gratefully acknowledged.

Author information

Affiliations

  1. Institute of Biochemistry and Clinical Biochemistry, Catholic University of Sacred Heart, Largo F. Vito 1, 00168, Rome, Italy

    F. Perri, F. Romitelli, F. Rufini, E. Di Stasio & B. Giardina

  2. CSS Hospital, IRCCS, Viale dei Cappuccini, 71013, San Giovanni Rotondo, FG, Italy

    F. Romitelli

  3. C.N.R. – I.C.R.M, Via Mario Bianco 9, 20131, Milan, Italy

    F. Secundo

  4. C.N.R. – I.C.R.M. c/o Institute of Biochemistry and Clinical Biochemistry, Catholic University, L.go F. Vito 1, 00168, Rome, Italy

    B. Giardina & A. Vitali

Authors
  1. F. Perri
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. F. Romitelli
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. F. Rufini
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. F. Secundo
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. E. Di Stasio
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. B. Giardina
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. A. Vitali
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to A. Vitali.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Perri, F., Romitelli, F., Rufini, F. et al. Different Structural Behaviors Evidenced in Thaumatin-Like Proteins: A Spectroscopic Study. Protein J 27, 13–20 (2008). https://doi.org/10.1007/s10930-007-9103-2

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10930-007-9103-2

Keywords

  • Unfolding
  • Intrinsic fluorescence
  • Circular dichroism
  • Thaumatin-like protein