Applications of nucleic acid chaperone activity of CspA and its homologues

Sangita Phadtare, Ling Zhu, Takashi Uemori, Hiroyuki Mukai, Ikunoshin Kato, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


In Escherichia coli, the cold shock response is exerted upon temperature change from 37 to 15°C and is characterized by induction of several cold shock proteins including its major cold shock protein, CspA. E. coli CspA family consists of nine members, CspA to CspI. CspA and some of its homologues play a critical role in cold acclimation of cells as RNA chaperones by destabilizing secondary structures in RNAs. Here, we showed that the nucleic acid melting activity of Csp proteins can be used to facilitate reactions, such as RT-PCR or RNA cleavage reactions by endoribonucleases, which are hindered by presence of secondary structures in the DNA/RNA substrate used. The low substrate specificity of Csps together with their compatibility with various enzymes and their stability and activity over a broad temperature range makes them ideal candidates to be used for a variety of processes.

Original languageEnglish (US)
Pages (from-to)110-117
Number of pages8
JournalJournal of molecular microbiology and biotechnology
Issue number3
StatePublished - Sep 2009

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Microbiology
  • Applied Microbiology and Biotechnology
  • Molecular Biology


  • CspA homologue
  • CspA protein
  • Nucleic acid melting
  • RNA chaperone


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