Advertisement

Controlled Assembly of the Filamentous Chaperone Gamma-Prefoldin into Defined Nanostructures

  • Douglas S. Clark
  • Dominic J. Glover
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1798)

Abstract

Self-assembling protein templates have enormous potential for the fabrication of multifunctional nanostructures that require precise positioning of individual molecules, such as enzymes and inorganic moieties, in regular patterns. A recently described approach uses ultrastable filaments composed of the gamma-prefoldin (γPFD) protein and engineered connector proteins to construct novel architectures useful for basic research and practical applications in nanobiotechnology. Here we describe the production of the γPFD and connector proteins from E. coli, and the assembly of γPFD with connector proteins into macromolecular structures with defined shapes.

Key words

Filament Protein Self-assembly Biomaterials Prefoldin Template Nanomaterials 

Notes

Acknowledgments

We are grateful to Samuel Lim for reviewing the manuscript and making helpful suggestions. This work was supported by the Air Force Office of Scientific Research (FA9550-14-1-0026).

References

  1. 1.
    Oh D, Qi J, Lu Y-C et al (2013) Biologically enhanced cathode design for improved capacity and cycle life for lithium-oxygen batteries. Nat Commun 4:2756CrossRefPubMedPubMedCentralGoogle Scholar
  2. 2.
    Abe S, Ueno T (2015) Design of protein crystals in the development of solid biomaterials. RSC Adv 5(27):21366–21375CrossRefGoogle Scholar
  3. 3.
    Bruns N, Pustelny K, Bergeron LM et al (2009) Mechanical nanosensor based on FRET within a thermosome: damage-reporting polymeric materials. Angew Chem Int Ed Engl 48(31):5666–5669CrossRefPubMedGoogle Scholar
  4. 4.
    Glover DJ, Clark DS (2016) Protein calligraphy: a new concept begins to take shape. ACS Cent Sci 2(7):438–444CrossRefPubMedPubMedCentralGoogle Scholar
  5. 5.
    Luo Q, Hou C, Bai Y et al (2016) Protein assembly: versatile approaches to construct highly ordered nanostructures. Chem Rev 116(22):13571–13632CrossRefPubMedGoogle Scholar
  6. 6.
    Whitehead TA, Boonyaratanakornkit BB, Höllrigl V et al (2007) A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii. Protein Sci 16(4):626–634CrossRefPubMedPubMedCentralGoogle Scholar
  7. 7.
    Glover DJ, Giger L, Kim SS et al (2016) Geometrical assembly of ultrastable protein templates for nanomaterials. Nat Commun 7:11771CrossRefPubMedPubMedCentralGoogle Scholar
  8. 8.
    Glover DJ, Giger L, Kim JR et al (2013) Engineering protein filaments with enhanced thermostability for nanomaterials. Biotechnol J 8(2):228–236CrossRefPubMedGoogle Scholar
  9. 9.
    Glover DJ, Clark DS (2015) Oligomeric assembly is required for chaperone activity of the filamentous γ-prefoldin. FEBS J 282(15):2985–2997CrossRefPubMedGoogle Scholar
  10. 10.
    Whitehead TA, Meadows AL, Clark DS (2008) Controlling the self-assembly of a filamentous hyperthermophilic chaperone by an engineered capping protein. Small 4(7):956–960CrossRefPubMedGoogle Scholar
  11. 11.
    Litowski JR, Hodges RS (2002) Designing heterodimeric two-stranded alpha-helical coiled-coils. Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity. J Biol Chem 277(40):37272–37279CrossRefPubMedGoogle Scholar
  12. 12.
    Bhardwaj A, Walker-Kopp N, Wilkens S et al (2008) Foldon-guided self-assembly of ultra-stable protein fibers. Protein Sci 17(9):1475–1485CrossRefPubMedPubMedCentralGoogle Scholar
  13. 13.
    Scopes RK (1974) Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 59(1):277–282CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Chemical and Biomolecular EngineeringUniversity of CaliforniaBerkeleyUSA
  2. 2.School of Biotechnology and Biomolecular SciencesThe University of New South WalesSydneyAustralia

Personalised recommendations