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The Journal of Experimental Biology 205, 2231-2236 (2002)
© 2002 The Company of Biologists Limited

Review

Temperature plasticity of contractile proteins in fish muscle

Shugo Watabe

Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan

e-mail: awatabe{at}mail.ecc.u-tokyo.ac.jp

Accepted 13 May 2002

Three myosin heavy chain isoforms with different actin-activated Mg²⁺-ATPase activities were found in the fast skeletal muscle from carp (Cyprinus carpio) acclimated to 10 and 30°C. The composition of three types of myosin heavy chain was dependent on acclimation temperature, demonstrating the presence of temperature-specific myosin isoforms in carp. Subsequently, the temperature-dependence of the sliding velocity of fluorescent F-actin in myosins isolated from 10°C- and 30°C-acclimated carp was measured. At 8°C, the filament velocity was three times higher for myosin from 10°C- than from 30°C-acclimated fish. Activation energies (E_a) for the sliding velocity of F-actin were 63 and 111 kJ mol^-1 for myosins from 10°C- and 30°C-acclimated fish, respectively. Activation energy for actin-activated Mg²⁺-ATPase activity was 0.46 kJ mol^-1 in myosin from 10°C-acclimated fish and 0.54 kJ mol^-1 in myosin from 30°C-acclimated fish. The inactivation rate constant (K_D) of Ca²⁺-ATPase was 7.5x10^-4s^-1 at 30°C for myosin from 10°C-acclimated fish, which was approximately twice that for myosin from 30°C-acclimated fish. It is suggested that these differences in thermostability reflect a more flexible structure of the myosin molecule in cold-acclimated carp, which results in a reduced activation enthalpy for contraction and, hence, a higher sliding velocity at low temperatures. Structural analysis of cDNAs encoding the carp myosin heavy chain demonstrated striking differences in two surface loops of myosin subfragment-1 (S1), loops 1 and 2, between the 10°C and 30°C types, which were predominantly expressed in carp acclimated to 10°C and 30°C, respectively. Chimeric myosins composed of Dictyostelium discoideum myosin backbones with loop sequences of carp S1 heavy chain isoforms demonstrated that the diversity of the loop 2 sequence of carp S1 affected the V_max of actin-activated Mg²⁺-ATPase activity.

Key words: actin-activated Mg²⁺-ATPase activity, activation energy, carp, Cyprinus carpio, chimeric myosin, Dictyostelium discoideum, inactivation rate constant, myosin, myosin heavy chain isoform, sliding velocity, subfragment-1, thermal acclimation, thermostability

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