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J. Biol. Chem., Vol. 276, Issue 6, 3911-3919, February 9, 2001

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Low Temperature Molecular Adaptation of the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca²⁺-ATPase 1 (SERCA 1) in the Wood Frog (Rana sylvatica)^*

Leonard Dode^§¶, Kurt Van Baelen, Frank Wuytack, and William L. Dean^§**

From the  Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium and the  Department of Biochemistry and Molecular Biology, School of Medicine, University of Louisville, Louisville, Kentucky 40292

We have compared the primary sequence and enzymatic properties of the sarcoplasmic reticulum Ca²⁺-ATPases from a cold-tolerant frog Rana sylvatica with those of a closely related cold-intolerant frog, Rana clamitans. Sarcoplasmic reticulum isolated from leg muscles of both species contains a major protein (~100 kDa) that reacts with a monoclonal antibody against sarco(endo)plasmic reticulum Ca²⁺-ATPase type 1 (SERCA1). The apparent molecular mass of R. sylvatica SERCA1 is 115 kDa, whereas that of R. clamitans is 105 kDa. However, the deduced amino acid sequences obtained from cDNAs do not indicate a difference in molecular weight, thus suggesting post-translational protein modification of R. sylvatica SERCA1. Comparison of the temperature dependence of both ATP hydrolysis and Ca²⁺ transport indicates that R. sylvatica SERCA1 exhibits significantly lower activation energy below 20 °C and an ~2-fold greater Ca²⁺-ATPase activity near 0 °C. Furthermore, R. sylvatica SERCA1 exhibits simple Michaelis-Menten kinetics with ATP and Ca²⁺ as opposed to the two-site ATP kinetics and positive cooperativity with Ca²⁺ observed for R. clamitans and mammalian SERCA1s. Cooperativity has been linked to protein-protein interaction in SERCA1, and this property may be altered in R. sylvatica SERCA1. Primary sequence comparison shows that R. sylvatica SERCA1 exhibits seven unique amino acid substitutions, three of which are in the ATP binding domain. We also report for the first time the presence of alternative splicing in the frog, resulting in isoforms SERCA1a and SERCA1b. Thus, it appears that the low temperature muscle contractility of R. sylvatica can be explained partially by significant functional and structural differences in SERCA1.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AJ298901 for R. sylvatica and AJ298902 for R. clamitans SERCA1s.

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