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• W2072701417 abstract "Tropomyosin (Tm) consists of 7 quasiequivalent repeats known as “periods,” and its specific function may be associated with these periods. To test the hypothesis that either period 2 or 3 promotes force generation by inducing a positive allosteric effect on actin, we reconstituted the thin filament with mutant Tm in which either period 2 (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>2Tm) or period 3 (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>3Tm) was deleted. We then studied: isometric tension, stiffness, 6 kinetic constants, and the pCa-tension relationship. N-terminal acetylation of Tm did not cause any differences. The isometric tension in<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>2Tm remained unchanged, and was reduced to ~60% in<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>3Tm. Although the kinetic constants underwent small changes, the occupancy of strongly attached cross-bridges was not much different. The Hill factor (cooperativity) did not differ significantly between<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>2Tm (1.79<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.19) and the control (1.73<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.21), or<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>3Tm (1.35<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.22) and the control. In contrast, p<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mrow><mml:mn>50</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math>decreased slightly in<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>2Tm (5.11<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.07), and increased significantly in<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi></mml:math>3Tm (5.57<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.09) compared to the control (5.28<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>±</mml:mo></mml:math>0.04). These results demonstrate that, when ions are present at physiological concentrations in the muscle fiber system, period 3 (but not period 2) is essential for the positive allosteric effect that enhances the interaction between actin and myosin, and increases isometric force of each cross-bridge." @default.
• W2072701417 created "2016-06-24" @default.
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• W2072701417 date "2009-10-13" @default.
• W2072701417 modified "2023-10-16" @default.
• W2072701417 title "Tropomyosin Period 3 Is Essential for Enhancement of Isometric Tension in Thin Filament-Reconstituted Bovine Myocardium" @default.
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• W2072701417 doi "https://doi.org/10.1155/2009/380967" @default.
• W2072701417 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2814127" @default.
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