NDLI: 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

Content Provider	Springer Nature Link
Author	Squerzanti, Monica Cervellati, Carlo Ura, Blendi Mischiati, Carlo Pucci, Piero Annunziata, Stefa Ianne, Carla Casadio, Rita Bergamini, Carlo M. Esposito, Carla
Copyright Year	2011
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.
Starting Page	227
Ending Page	234
Page Count	8
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	44
Issue Number	1
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2011-11-16
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Transglutaminase Skeletal troponin T Protein post-translational modification Biochemistry Analytical Chemistry Biochemical Engineering Life Sciences Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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