The self-association of basic helix-loop-helix peptides

  • H. Wendt
  • R. M. ThomasEmail author
Biological Systems
Part of the Progress in Colloid & Polymer Science book series (PROGCOLLOID, volume 107)


As part of a study into the homo- and hetero-oligomerization properties of muscle-specific transcriptional factors, and their interation with DNA, sedimentation equilibrium studies, accompanied by circular dichroism measurements, have been made on peptides derived from the helix-loop-helix regions of MyoD and E47. In addition, a chimeric peptide, in which residues from the loop region of E47 were substituted into that of MyoD, a fluorescently labelled derivative of the MyoD-bHLH peptide and a disulphide crosslinked version of MyoD-bHLH have also been investigated. MyoD-bHLH has been found to form a monomer tetramer equilibrium in the µM concentration range, while E47-bHLH exists as a highly associated dimer. The MyoD-bHLH derivatives appear to exhibit the same oligomerization behavior as their MyoD-bHLH parent. CD studies of the disulphide-crosslinked peptide show that a level of organization higher than that of the dimer is required for structural stability in the MyoD-bHLH system. The rôle of self-association in the context of the biological function of these peoteins is discussed.

Key words

Helix-loop-helix peptides self-association sedimentation equilibrium circular dichroism 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Thomas RM, Wendt H, Zampieri A, Bosshard HR (1996) Colloid Polym Sci 99:24–30CrossRefGoogle Scholar
  2. 2.
    Thomas RM, Zampieri A, Jumel K, Harding SE (1997) Eur Biophys J 25:405–410PubMedCrossRefGoogle Scholar
  3. 3.
    Davis RL, Weintraub H (1992) Science 256:1027–1030PubMedCrossRefGoogle Scholar
  4. 4.
    Weintraub H (1993) Cell 75:1241–1244PubMedCrossRefGoogle Scholar
  5. 5.
    Caudy M, Vassin H, Brand M, Tuma R, Jan LY, Jan YN (1988) Cell 55:1061–1067PubMedCrossRefGoogle Scholar
  6. 6.
    Cabrera CV, Alonso MC (1991) EMBO J 10:2965–2973PubMedGoogle Scholar
  7. 7.
    Weintraub H, Davis RL, Tapscott S, Thayer M, Krause M, Benazra R, Blackwell TK, Turner D, Rupp R, Hollenberg S, Zhuang Y, Lassar A (1991) Science 251:761–766PubMedCrossRefGoogle Scholar
  8. 8.
    Weintraub H (1993) Cell 75:1241–1244PubMedCrossRefGoogle Scholar
  9. 9.
    Olson EN, Klein WH (1994) Genes Dev 8:1–8PubMedCrossRefGoogle Scholar
  10. 10.
    Murre C, McCaw PS, Baltimore D (1989) Cell 56:777–783PubMedCrossRefGoogle Scholar
  11. 11.
    Lassar A, Davis RL, Wright WE, Kadesch T, Murre C, Voronova A, Baltimore D, Weintraub H (1991) Cell 66:305–315PubMedCrossRefGoogle Scholar
  12. 12.
    Blackwell TK, Weintraub H (1990) Science 250:1104–1110PubMedCrossRefGoogle Scholar
  13. 13.
    Ma PCM, Rould MA, Weintraub H, and Pabo CO (1994) Cell, 77:451–459PubMedCrossRefGoogle Scholar
  14. 14.
    Ellenberger T, Fass D, Arnaud M, and Harrison SC (1994) Genes Dev 8:970–980PubMedCrossRefGoogle Scholar
  15. 15.
    Anthony-Cahill SJ, Benfield PA, Fairman R, Wasserman ZR, Brenner SL, Stafford WF, Altenbach C, Hubbell WL, DeGrado WF (1992) Science 255:979–983PubMedCrossRefGoogle Scholar
  16. 16.
    Fairman R, Beran-Steed RK, Anthony-Cahill SJ, Lear JD, Stafford WF, DeGrado WF, Benfield PA, Brenner SL (1993) Proc Natl Acad Sci 90:10429–10433PubMedCrossRefGoogle Scholar
  17. 17.
    Studier FW, Moffat BA (1986) J Mol Biol 189:113–130PubMedCrossRefGoogle Scholar
  18. 18.
    Laue TM, Shah B, Ridgeway TM and Pelletier SL (1992) In: Harding SE, Rowe AJ, Horton JC (eds), Analytical Ultracentrifugation in Biochemistry and Polymer Science. Royal Society of Chemistry, Cambridge, U.K.Google Scholar
  19. 19.
    Laue TM, Starovasnik MA, Weintraub H, Sun X-H, Snider L, Klevit RE (1995) Proc Natl Acad Sci 92:11824–11828PubMedCrossRefGoogle Scholar
  20. 20.
    Starovasnik, MA, Blackwell TK, Laue TM, Weintraub H, Klevit RE (1992) Biochemistry 31:9891–9903PubMedCrossRefGoogle Scholar
  21. 21.
    Benezra R, Davis RL, Lockshorn D, Turner DL, Weintraub H (1990) Cell 61:49–59PubMedCrossRefGoogle Scholar
  22. 22.
    Sun XH, Copeland NG, Jenkins NA, Baltimore D (1991) Mol Cell Biol 11:5603–5611PubMedGoogle Scholar
  23. 23.
    Wilson RB, Megerditch K, Shen C, Benezra R, Zwollo P, Dymecki SM, Desiderio SV, Kadesch T (1991) Mol Cell Biol 11:6185–6191PubMedGoogle Scholar
  24. 24.
    Jen Y, Weintraub H, Benezra R (1992) Genes Dev 6:1466–1479PubMedCrossRefGoogle Scholar
  25. 25.
    Sun XH, Baltimore D (1991) Cell 64:459–470PubMedCrossRefGoogle Scholar
  26. 26.
    Matallo SJ, Schepartz A (1997) Nat Struct Biol 4:115–117CrossRefGoogle Scholar

Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG 1997

Authors and Affiliations

  1. 1.Department of Biological Chemistry and Molecular PharmacologyHarvard Medical SchoolBostonUSA
  2. 2.Institut für PolymereETH-ZentrumZürichSwitzerland

Personalised recommendations