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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

View larger version (13K): [in a new window]   Fig. 1. Structural flexibility and functional differences of myosin isoforms from thermally acclimated carp. (A) A plot of relative Ca2+-ATPase activity versus incubation time (modified from Watabe et al., 1992) from which the inactivation rate constant (KD) can be derived. (B) Arrhenius plot of the sliding velocity of F-actin on myosin (modified from Chaen et al., 1996) from which the activation energy (Ea) for sliding velocity can be derived. (C) Arrhenius plot of actin-activated Mg2+-ATPase activity (modified from Watabe et al., 1992) from which the Ea for actin-activated Mg2+-ATPase can be derived. Myosin isoforms were prepared from carp acclimated to 10°C (open circles) and 30°C (filled circles).

View larger version (35K): [in a new window]   Fig. 2. Amino acid sequences around loops 1 (A) and 2 (B) in the 10°C, intermediate (I) and 30°C types of S1 heavy chain from carp (modified from Hirayama et al., 2000) and in S1 heavy chains of chicken myosin from a variety of tissues. The two loops are boxed.