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Wintering Sasa senanensis, dwarf bamboo, is known to employ deep supercooling as the mechanism of cold hardiness in most of its tissues from leaves to rhizomes. The breakdown of supercooling in leaf blades has been shown to proceed in a random and scattered manner with a small piece of tissue surrounded by longitudinal and transverse veins serving as the unit of freezing. The unique cold hardiness mechanism of this plant was further characterized using current year leaf blades. Cold hardiness levels (LT20: the lethal temperature at which 20% of the leaf blades are injured) seasonally increased from August (−11°C) to December (−20°C). This coincided with the increases in supercooling capability of the leaf blades as expressed by the initiation temperature of low temperature exotherms (LTE) detected in differential thermal analyses (DTA). When leaf blades were stored at −5°C for 1–14 days, there was no nucleation of the supercooled tissue units either in summer or winter. However, only summer leaf blades suffered significant injury after prolonged supercooling of the tissue units. This may be a novel type of low temperature-induced injury in supercooled state at subfreezing temperatures. When winter leaf blades were maintained at the threshold temperature (−20°C), a longer storage period (1–7 days) increased lethal freezing of the supercooled tissue units. Within a wintering shoot, the second or third leaf blade from the top was most cold hardy and leaf blades at lower positions tended to suffer more injury due to lethal freezing of the supercooled units. LTE were shifted to higher temperatures (2–5°C) after a lethal freeze-thaw cycle. The results demonstrate that the tissue unit compartmentalized with longitudinal and transverse veins serves as the unit of supercooling and temperature- and time-dependent freezing of the units is lethal both in laboratory freeze tests and in the field. To establish such supercooling in the unit, structural ice barriers such as development of sclerenchyma and biochemical mechanisms to increase the stability of supercooling are considered important. These mechanisms are discussed in regard to ecological and physiological significance in winter survival.

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The 78-kDa glucose regulated protein (GRP78), a member of stress proteins, was cloned from a cDNA library of Japanese oyster Crassostrea gigas. The analysis on Japanese oyster GRP78 clone of approximately 2.6 kb revealed that the entire open reading frame was 1983 bp long and encoded 661 amino acid residues. At the DNA sequence level, the coding region of Japanese oyster GRP78 gene was 72, 62, and 62% identical to those of chicken GRP78, Japanese flounder HSP70, and Japanese flounder HSC71 genes, respectively. Deduced amino acid sequence of Japanese oyster GRP78 was 84, 62, and 62% identical to those of chicken GRP78, Japanese flounder HSP70, and Japanese flounder HSC71, respectively. Japanese oyster GRP78 contained an 18-residue sequence at the N-terminus that exhibits characteristics of a cleavable signal sequence. It also contained an ATPase domain, and a peptide-binding domain in addition to a Lys-Asp-Glu-Leu (KDEL) peptide motif that is involved in determining endoplasmic reticulum localization. Northern blot analysis showed that GRP78 mRNA was induced with heatshock treatment in the oyster tissues.