Thesis - University Access Only
Master of Science (MS)
Department / School
Cold-regulation specific cDNA pHVCR2001 was isolated by a previous graduate student Chang (1993). The deduced amino acid sequence of HVCR2001 revealed a N-terminal signal peptide and a single hydrophobic transmembrane domain near the C-terminus. In vitro translation system with dog pancreatic microsomal membrane was employed [sic] to determine that HVCR2001 protein is a putative transmembrane protein processed through a secretory pathway. Results from in vitro translation reactions showed a smaller product in the presence of microsomal membrane compared to the product in the absence of microsomal membrane, and the size of this product was close to predicted theoretical [sic] molecular mass. This indicated that the protein was inserted into microsomal membrane in a process in which the signal peptide had been removed. The function of this putative membrane protein played in cold acclimation process is not known. The decay of HVCR2001 message in vivo at 2 C or 25 C was also investigated in this study. The first set of result showed that low temperature stabilized HVCR2001 message, which meant, post-transcriptional level of regulation contributed to the accumulation of this message at low temperature. However, the result of the repeated experiment did not quite support [sic] the first one. More repeats of this experiment are necessary to be carried out to verify the first set of result.
Library of Congress Subject Headings
Plants -- Frost resistance
Proteins -- Metabolism
South Dakota State University
Yang, Fei, "Cold-Regulation Specific Gene HVCR2001 Encodes a Putative Integral Transmembrane Protein" (1996). Electronic Theses and Dissertations. 233.