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    Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin

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    Author
    Mathur, Mohit C.; Kobayashi, Tomoyoshi; Chalovich, Joseph
    Abstract
    Alterations in the troponin complex can lead to increases or decreases in contractile activity. Most mutations of troponin that cause hypertrophic cardiomyopathy increase the activity of cardiac muscle fibers. In at least some cases these mutants stabilize the active state of regulated actin. In contrast, phosphorylation of troponin I at residues 43, 45, and 144 inhibits muscle contractility. To determine if alterations of troponin I that reduce activity do stabilize the inactive state of actin, we introduced negative charges at residues 43, 45, and 144 of troponin I to mimic a constitutively phosphorylated state. At saturating calcium, all mutants decreased ATPase rates relative to wild-type actin-tropomyosin-troponin. Reduced activation of ATPase activity was seen with a single mutation at S45E and was not further altered by mutating the other two sites. In the presence of low concentrations of NEM-S1, wild-type troponin was more active than the mutants. At high NEM-S1, the rates of wild-type and mutants approached the same limiting value. Changes in Ca21 affinity also support the idea that the equilibrium between states of actin-tropomyosin-troponin was shifted to the inactive state by mutations that mimic troponin I phosphorylation. Originally published Biophysical Journal, Vol. 94, No. 2, Jan. 2008
    URI
    http://hdl.handle.net/10342/3051
    Subject
     Troponin complex; Actin stabilization; Cardiac muscle fibers 
    Date
    2008-01-15
    Citation:
    APA:
    Mathur, Mohit C., & Kobayashi, Tomoyoshi, & Chalovich, Joseph. (January 2008). Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin. Biophysical Journal, 94(2), 542- 549. Retrieved from http://hdl.handle.net/10342/3051

    Display/Hide MLA, Chicago and APA citation formats.

    MLA:
    Mathur, Mohit C., and Kobayashi, Tomoyoshi, and Chalovich, Joseph. "Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin". Biophysical Journal. 94:2. (542-549), January 2008. September 26, 2023. http://hdl.handle.net/10342/3051.
    Chicago:
    Mathur, Mohit C. and Kobayashi, Tomoyoshi and Chalovich, Joseph, "Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin," Biophysical Journal 94, no. 2 (January 2008), http://hdl.handle.net/10342/3051 (accessed September 26, 2023).
    AMA:
    Mathur, Mohit C., Kobayashi, Tomoyoshi, Chalovich, Joseph. Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin. Biophysical Journal. January 2008; 94(2): 542-549. http://hdl.handle.net/10342/3051. Accessed September 26, 2023.
    Collections
    • Biochemistry and Molecular Biology
    Publisher
    East Carolina University

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