Recent developments in bacterial cold-shock response

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)125-136
Number of pages12
JournalCurrent Issues in Molecular Biology
Volume6
Issue number2
StatePublished - Jul 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Microbiology (medical)

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