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 language | English |
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Pages (from-to) | 227-234 |
Number of pages | 8 |
Journal | Amino Acids |
Volume | 44 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jan 2013 |
Keywords
- Protein post-translational modification
- Skeletal troponin T
- Transglutaminase
ASJC Scopus subject areas
- Biochemistry
- Clinical Biochemistry
- Organic Chemistry