A peptide derived from pICln induced a strong hypotonic resistance in Escherichia coli cells.
We demonstrated previously that expression of rat pICln in Escherichia coli conferred a strong resistance to hypotonic stress. To define the intramolecular functional domain responsible for the resistance, molecular dissection of pICln was performed and the obtained peptides were expressed in E. coli. The cells expressing the peptides were exposed to a hypotonic solution, and their 'survival rates' were observed. The cells expressing only the peptides including the second acidic domain of pICln exhibited significantly higher 'survival rates' after hypotonic stress. The functional domain against hypotonicity was finally narrowed down to a peptide consisting of a 46-amino acid residue, P107-152. We conclude that the expression of P107-152 in E. coli cells could enhance their resistance to a hypotonic environment.
Tao
G Z
GZ
Department-2 of Biochemistry, School of Medicine, Akita University, Hondo 1-1-1, Akita, 010-8543, Japan. tgz@med.akita-u.ac.jp
Tashima
Y
Y
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D018118:Chloride Channels / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D003001:Cloning, Molecular; D015169:Colony Count, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D007038:Hypotonic Solutions / Q000494:pharmacology; D007473:Ion Channels / Q000037:antagonists & inhibitors; D009997:Osmotic Pressure; D010455:Peptides / Q000378:metabolism / Q000502:physiology*; D016133:Polymerase Chain Reaction; D017434:Protein Structure, Tertiary; D051381:Rats
D018118:Chloride Channels; C498729:Clns1a protein, rat; D007038:Hypotonic Solutions; D007473:Ion Channels; D010455:Peptides; D000255:Adenosine Triphosphate; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid