Skip to main content
SpringerLink
Log in

Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

Dehydrins are a class of stress proteins that belong to the family of Late Embryogenesis Abundant (LEA) proteins in plants, so named because they are highly expressed in late stages of seed formation. In somatic cells, their expression is very low under normal conditions, but increases critically upon dehydration elicited by water stress, high salinity or cold. Dehydrins are thought to be intrinsically disordered proteins, which represents a challenge in understanding their structure–function relationship. Herein we present the backbone 1H, 15N and 13C NMR assignment of the 185 amino acid long ERD14 (Early Response to Dehydration 14), which is a K3S-type, typical dehydrin of A. thaliana. Secondary chemical shifts as well as NMR relaxation data show that ERD14 is fully disordered under near native conditions, with short regions of somewhat restricted motion and 5–25% helical propensity. These results suggest that ERD14 may have partially preformed elements for functional interaction with its partner(s) and set the stage for further detailed structural and functional studies of ERD14 both in vitro and in vivo.

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

Similar content being viewed by others

References

  • Aswad DW, Paranandi MV, Schurter BT (2000) Isoaspartate in peptides and proteins: formation, significance, and analysis. J Pharm Biomed Anal 21:1129–1136

    Article  Google Scholar 

  • Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K (2005) NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophys J 88:2030–2037

    Article  Google Scholar 

  • Braun D, Wider G, Wüthrich K (1994) Sequence-corrected 15N “random coil” chemical shifts. J Am Chem Soc 116:8466–8469

    Article  Google Scholar 

  • Chatterjee A, Kumar A, Chugh J, Srivastava S, Bhavesh N, Hosur R (2005) NMR of unfolded proteins. J Chem Sci 117:3–21

    Article  Google Scholar 

  • Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97:795–803

    Article  ADS  Google Scholar 

  • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104:3607–3622

    Article  Google Scholar 

  • Findlater EE, Graether SP (2009) NMR assignments of the intrinsically disordered K2 and YSK2 dehydrins. Biomol NMR Assignments 3:273–275

    Article  Google Scholar 

  • Fuxreiter M, Simon I, Friedrich P, Tompa P (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 338:1015–1026

    Article  Google Scholar 

  • Fuxreiter M, Tompa P, Simon I (2007) Structural disorder imparts plasticity on linear motifs. Bioinformatics 23:950–956

    Article  Google Scholar 

  • Goddard TD, Kneller DG SPARKY 3. University of California, San Francisco. http://www.cgl.ucsf.edu/home/sparky/

  • Hundertmark M, Hincha DK (2008) LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 9:118

    Article  Google Scholar 

  • Keller RLJ (2004) The computer aided resonance assignment tutorial. CANTINA Verlag, Goldau, Switzerland

    Google Scholar 

  • Kim S, Nam K (2010) Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. Plant Cell Rep 29:203–209

    Article  Google Scholar 

  • Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K (1994a) Cloning of cDNAs for genes that are early-responsive to dehydration stress (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP cognate genes. Plant Mol Biol 25:791–798

    Article  Google Scholar 

  • Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K (1994b) Characterization of two cDNAs (ERD10 and ERD14) corresponding to genes that respond rapidly to dehydration stress in Arabidopsis thaliana. Plant Cell Physiol 35:225–231

    Google Scholar 

  • Kovacs D, Kalmar E, Torok Z, Tompa P (2008a) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol 147:381–390

    Article  Google Scholar 

  • Kovacs D, Agoston B, Tompa P (2008b) Disordered plant LEA proteins as molecular chaperones. Plant Signaling Behav 3:710–713

    Article  Google Scholar 

  • Löhr F, Rüterjans H (1998) Detection of nitrogen-nitrogen J-couplings in proteins. J Magn Reson 132:130–137

    Article  Google Scholar 

  • Löhr F, Pfeiffer S, Lin Y, Hartleib J, Klimmek O, Rüterjans H (2000) HNCAN pulse sequences for sequential backbone resonance assignment across proline residues in perdeuterated proteins. J Biomol NMR 18:337–346

    Article  Google Scholar 

  • Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71–75

    Article  Google Scholar 

  • Mohan A, Oldfield CJ, Radivojac P, Vacic V, Cortese MS, Dunker AK, Uversky VN (2006) Analysis of molecular recognition features (MoRFs). J Mol Biol 362:1043–1059

    Article  Google Scholar 

  • Nylander M, Svensson J, Palva ET, Welin BV (2001) Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana. Plant Mol Biol 45:263–279

    Article  Google Scholar 

  • Rorat T (2006) Plant dehydrins–tissue location, structure and function. Cell Mol Biol Lett 11:536–556

    Article  Google Scholar 

  • Shinozaki K, Yamaguchi-Shinozaki K (1996) Molecular responses to drought and cold stress. Curr Opin Biotechnol 7:161–167

    Article  Google Scholar 

  • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527–533

    Article  Google Scholar 

  • Tompa P (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579:3346–3354

    Article  Google Scholar 

  • Tompa P (2009) Structure and function of intrinsically disordered proteins. CRC Press, Boca Raton

    Book  Google Scholar 

  • Tompa P, Kovacs D (2010) Intrinsically disordered chaperones in plants and animals. Biochem Cell Biol 88:167–174

    Article  Google Scholar 

  • Tompa P, Szasz C, Buday L (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30:484–489

    Article  Google Scholar 

  • Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K (2006) Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 91:2243–2249

    Article  Google Scholar 

  • Uversky VN (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11:739–756

    Article  Google Scholar 

  • Welin BV, Olson A, Nylander M, Palva ET (1994) Characterization and differential expression of dhn/lea/rab-like genes during cold acclimation and drought stress in Arabidopsis thaliana. Plant Mol Biol 26:131–144

    Article  Google Scholar 

  • Wishart DS, Bigam CG, Holm A, Hodges RS, Sykes BD (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67–81

    Article  Google Scholar 

  • Wright PE, Dyson HJ (2009) Linking folding and binding. Curr Opin Struct Biol 19:31–38

    Article  Google Scholar 

Download references

Acknowledgments

This research was supported by the grant of the Hungarian Scientific Research Fund (OTKA; NK71582, K72973 and NI-68466) and ICGEB (CRP/HUN08-03). The European Union and the European Social Fund have provided financial support to the project under the grant agreement no. TÁMOP 4.2.1./B-09/KMR-2010-0003. Financial support by the Access to Research Infrastructures activity in the 6th Framework Programme of the EC (Contract # RII3-026145, EU-NMR), the technical assistance with and the measurements of the NMR spectra by F. Löhr are also gratefully acknowledged.

Author information

Authors and Affiliations

  1. Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina út 29., 1113, Budapest, Hungary

    Bianka Szalainé Ágoston, Dénes Kovács & Péter Tompa

  2. Protein Modelling Group, Hungarian Academy of Sciences and Eötvös Loránd University, Pázmány P. s. 1/A., 1117, Budapest, Hungary

    András Perczel

  3. Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány P. s. 1/A., 1117, Budapest, Hungary

    András Perczel

Authors
  1. Bianka Szalainé Ágoston
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Dénes Kovács
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Péter Tompa
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. András Perczel
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to András Perczel.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Szalainé Ágoston, B., Kovács, D., Tompa, P. et al. Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14. Biomol NMR Assign 5, 189–193 (2011). https://doi.org/10.1007/s12104-011-9297-2

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-011-9297-2

Keywords

Search

Navigation