The side chain of glutamine 13 is the acyl-donor amino acid modified by type 2 transglutaminase in subunit T of the native rabbit skeletal muscle troponin complex

Monica Squerzanti, Carlo Cervellati, Blendi Ura, Carlo Mischiati, Piero Pucci, Stefano Annunziata, Carla Iannone, Rita Casadio, Carlo M. Bergamini, Carla Esposito

Research output: Contribution to journalArticle

Abstract

Subunit T of the native muscle troponin complex is a recognised substrate of transglutaminase both in vitro and in situ with formation of isopeptide bonds. Using a proteomic approach, we have now determined the precise site of in vitro labelling of the protein. A preparation of troponin purified from ether powder from mixed rabbit skeletal muscles was employed as transglutaminase substrate. The only isoform TnT2F present in our preparation was recognised as acyl-substrate by human type 2 transglutaminase which specifically modified glutamine 13 in the N-terminal region. During the reaction, the troponin protein complex was polymerized. Results are discussed in relation to the structure of the troponin T subunit, in the light of the role of troponins in skeletal and cardiac muscle diseases, and to the rules governing glutamine side chain selection by tissue transglutaminase.

Original languageEnglish
Pages (from-to)227-234
Number of pages8
JournalAmino Acids
Volume44
Issue number1
DOIs
Publication statusPublished - Jan 2013

Keywords

  • Protein post-translational modification
  • Skeletal troponin T
  • Transglutaminase

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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    Squerzanti, M., Cervellati, C., Ura, B., Mischiati, C., Pucci, P., Annunziata, S., Iannone, C., Casadio, R., Bergamini, C. M., & Esposito, C. (2013). The side chain of glutamine 13 is the acyl-donor amino acid modified by type 2 transglutaminase in subunit T of the native rabbit skeletal muscle troponin complex. Amino Acids, 44(1), 227-234. https://doi.org/10.1007/s00726-011-1144-3