Abstract

The temperature-dependent expression of lactate dehydrogenase-B (LDH-B) was compared between two environmentally distinct populations of Fundulus heteroclitus acclimated to 10 degrees C and 20 degrees C. The variability in LDH-B protein expression both within and between populations is consistent with a model of thermal compensation. The northern population from the colder environment expresses a twofold greater amount of LDH-B protein than the warmer southern population at both acclimation temperatures. Correspondingly, both populations have 1.3-fold greater levels of the enzyme at an acclimation temperature of 10 degrees C in comparison to 20 degrees C. In 20 degrees C-acclimated individuals there is a similar twofold difference between populations for LDH-B mRNA concentrations, and LDH-B protein and mRNA are highly correlated (r = 0.81). After acclimation to 10 degrees C, this difference between populations is not seen and in the northern population there is no relationship between LDH-B mRNA and protein levels. Thus the molecular mechanism regulating LDH-B enzyme expression changes in response to temperature acclimation and is different between populations.

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