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Science 16 March 1990:
Vol. 247. no. 4948, pp. 1339 - 1341
DOI: 10.1126/science.2138356
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Articles

Science, Vol 247, Issue 4948, 1339-1341
Copyright © 1990 by American Association for the Advancement of Science

articles

Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments

T Tao, BJ Gong, and PC Leavis

Department of Muscle Research, Boston Biomedical Research Institute, MA 02114.

The role of troponin-I (the inhibitory subunit of troponin) in the regulation by Ca2+ of skeletal muscle contraction was investigated with resonance energy transfer and photo cross-linking techniques. The effect of Ca2+ on the proximity of troponin-I to actin in reconstituted rabbit skeletal thin filaments was determined. The distance between the cysteine residue at position 133 (Cys133) of troponin-I and Cys374 of actin increases by approximately 15 angstroms on binding of Ca2+ to troponin-C. Also, troponin-I labeled at Cys133 with benzophenone-4-maleimide could be photo cross-linked to actin in the absence of Ca2+, but not in its presence. These results suggest that troponin-I is attached to actin in the Ca2(+)-free or relaxed state of muscle, and that it detaches from actin on Ca2+ activation of contraction. Thus, troponin-I may function as a Ca2(+)-dependent molecular switch in regulation of skeletal muscle contraction.


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Phosphorylation Specificities of Protein Kinase C Isozymes for Bovine Cardiac Troponin I and Troponin T and Sites within These Proteins and Regulation of Myofilament Properties.
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Mapping the Functional Domains within the Carboxyl Terminus of alpha-Tropomyosin Encoded by the Alternatively Spliced Ninth Exon.
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Kinetic Studies of Calcium Binding to the Regulatory Site of Troponin C from Cardiac Muscle.
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NH(2)-terminal Truncation of Skeletal Muscle Troponin T Does Not Alter the Ca[IMAGE] Sensitivity of Thin Filament Assembly.
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Calcium-induced Troponin Flexibility Revealed by Distance Distribution Measurements between Engineered Sites.
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