Recent developments in bacterial cold-shock response.
In response to temperature downshift, a number of changes occur in cellular physiology such as, (i) decrease in membrane fluidity, (ii) stabilization of secondary structures of nucleic acids leading to reduced efficiency of mRNA translation and transcription, (iii) inefficient folding of some proteins, and (iv) hampered ribosome function. Cold-shock response and adaptation has been quite extensively studied in Escherichia coli and Bacillus subtilis. A number of cold shock proteins are induced to counteract these harmful effects of temperature downshift. General principles of cold-shock response along with recent findings on desaturase system, RNA chaperone and transcription antitermination function of CspA homologues, cold shock induction of chaperones and synthesis of trehalose, CspA homologues from hyperthermophilic bacteria and possible multiple roles of cold shock proteins in other stress responses of bacteria are discussed.
Phadtare
Sangita
S
Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, USA. phadtasa@umdnj.edu
D001407:Bacillus / Q000502:physiology; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000502:physiology; D003080:Cold Temperature; D000458:Cyanobacteria / Q000502:physiology; D044943:Fatty Acid Desaturases / Q000502:physiology; D018832:Molecular Chaperones / Q000502:physiology
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C062260:cold shock protein CS7.4, Bacteria; D044943:Fatty Acid Desaturases