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Am J Physiol Regul Integr Comp Physiol 281: R1374-R1379, 2001;
0363-6119/01 $5.00
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Vol. 281, Issue 5, R1374-R1379, November 2001

Translational initiation is uncoupled from elongation at 18°C during mammalian hibernation

Frank van Breukelen and Sandra L. Martin

Department of Cellular and Structural Biology, University of Colorado School of Medicine, Denver, Colorado 80262-B111

Cellular and organismal homeostasis must be maintained across a body temperature (Tb) range of 0 to 37°C during mammalian hibernation. Hibernators depress biosynthetic activities including protein synthesis, concordant with limited energy availability and temperature effects on reaction rates. We used polysome analysis to show that initiation of protein synthesis ceases during entrance into torpor in golden-mantled ground squirrels (Spermophilus lateralis) when Tb reaches 18°C. Elongation of preinitiated polypeptides continues slowly throughout the torpor bout. As Tb begins to rise, initiation resumes even at temperatures below 18°C, although the euthermic polysome pattern is not reestablished. At precisely 18°C, there is a large increase in initiation events and a complete restoration of euthermic polysome distribution patterns. These data indicate a role for both passive and active depression of translation during torpor and are consistent with a requirement for new protein biosynthesis during each interbout arousal.

protein synthesis; polyribosome; ribosome


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