A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization

Adriana A. Paulucci, Angela M. Katsuyama, Aurea D. Sousa, Chuck S. Farah

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Tropomyosin is a 284 residue dimeric coiled-coil protein that interacts in a head-to-tail manner to form linear filaments at low ionic strengths. Polymerization is related to tropomyosin's ability to bind actin, and both properties depend on intact N- and C-termini as well as α-amino acetylation of the N-terminus of the muscle protein. Nα- acetylation can be mimicked by an N-terminal Ala-Ser fusion in recombinant tropomyosin (ASTm) produced in Escherichia coli. Here we show that a recombinant tropomyosin fragment, corresponding to the protein's first 260 residues plus an Ala-Ser fusion [ASTm(1-260)], polymerizes to a much greater extent than the corresponding full-length recombinant protein, despite the absence of the C-terminal 24 amino acids. This polymerization is sensitive to ionic strength and is greatly reduced by the removal of the N-terminal Ala-Ser fusion [nfTm(1-260)]. CD studies show that nonpolymerizable tropomyosin fragments, which terminate at position 260 [Tm(167-260) and Tm(143-260)], as well as Tm(220-284), are able to interact with ASTm(1-142), a nonpolymerizable N-terminal fragment, and that the head-to-tail interactions observed for these fragment pairs are accompanied by a significant degree of folding of the C-terminal tropomyosin fragment. These results suggest that the new C-terminus, created by the deletion, polymerizes in a manner similar to the full-length protein. Head-to-tail binding for fragments terminating at position 260 may be explained by the presence of a greater concentration of negatively charged residues, while, at the same time, maintaining a conserved pattern of charged and hydrophobic residues found in polymerizable tropomyosins from a variety of sources.

Original languageEnglish (US)
Pages (from-to)589-600
Number of pages12
JournalEuropean Journal of Biochemistry
Issue number3
StatePublished - Feb 2004
Externally publishedYes


  • Circular dichroism
  • Head-to-tail interaction
  • Protein folding
  • Protein polymerization
  • Tropomyosin

ASJC Scopus subject areas

  • Biochemistry


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