A synthetic peptide mimics troponin I function in the calcium‐dependent regulation of muscle contraction

FEBS Letters

Rüegg, J.Casper²  Strauss, John D.²  Hodges, Robert S.¹  Van Eyk, Jennifer E.¹ 

[1] Department of Biochemistry and MRC Group in Protein Structure and Function, University of Alberta, Edmonton, AB, Canada;II Physiologisches Institut, University of Heidelberg, W-6900 Heidelberg, Germany

关键词: Troponin I;    Synthetic peptide;    Muscle regulation;    Protein-protein interaction;    A TP;    adenosine triphosphate;    DTE;    dithioerythritol;    DTT;    dithiothreitol;    EDTA;    ethylenediamine tetraacetic acid;    EGTA;    ethylene glycol (bis(β-aminoethylether) N;    N;    N';    N';    tetraacetic acid;    NADH;    nicotinamide adenine dinucleotide;    NaN3;    sodium azide;    S1;    myosin subfragment 1;    TM;    tropomyosin;    Tn;    troponin;    TnI;    troponin I;    TnT;    troponin T;    TnC;    troponin C;   

DOI  :  10.1016/0014-5793(93)81344-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new technique for treating skinned cardiac muscle fibers has been developed in which troponin I is extracted, giving rise to unregulated fibers. The effect of the 12-residue troponin I peptide on these fibers indicates that this region of troponin I is solely responsible for muscle relaxation (inhibition of force). Furthermore, troponin I peptide-troponin C reconstituted fibers are stable through several contraction-relaxation cycles indicating the peptide can switch binding sites between actin and troponin C. The troponin I peptide can substitute for the native protein as part of the calcium-sensitive molecular switch that controls muscle regulation.

【 授权许可】

Unknown