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Picture courtesy of
Center for Molecular Biophysics |
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Masayori Inouye Transmembrane Signal Transduction by Protein Histidine: Adaptive responses of E. coli to medium osmolarity provides and ideal system to study signal transduction across the membrane. Osmotic signals modulate the histidine kinase activity of EnvZ protein, a transmembrane osmosensor to phosphorylate OmpR protein, a transcriptional factor, which regulates the expression of two membrane proteins. Molecular genetical as well as biochemical and biophysical approaches are taken to elucidate the signal transduction mechanisms. Cold-shock Response and Adaptation: In nature, living organisms are constantly exposed to temperature changes. In contrast to heat-shock response, cold-shock response is not well understood. We have demonstrated that when E. coli cells are exposed to low temperature, a number of proteins called 'cold-shock proteins' are specifically induced. Among them, there are ribosome-associated proteins, which are required for protein synthesis at low temperature, and RNA/DNA chaperones, which are considered to play important roles in mRNA translation, transcription and DNA replication. We are attempting to elucidate how the gene expression for cold-shock proteins is regulated and what the functions are of individual cold-shock proteins. In addition to E. coli, we are also investigating how human cells respond to low temperature. Protein Folding: We are attempting to decipher the precise process of protein folding by molecular genetic as well as biochemical approaches using prosubtilisin as a model system. In this system, the propeptide of 77 amino acid residues function as an intramolecular chaperone which is essential for the folding of active subtilisin.
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