Applications of Nucleic Acid Chaperone Activity of CspA and Its Homologues
| Autor: | Sangita Phadtare, Ling Zhu, Masayori Inouye, Takashi Uemori, Hiroyuki Mukai, Ikunoshin Kato |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Escherichia coli Proteins
Physiology Biology medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Microbiology Substrate Specificity Stress Physiological Nucleic Acids Heat shock protein Endoribonucleases RNA chaperone Escherichia coli medicine Humans Chaperone activity Heat-Shock Proteins RNA-Directed DNA Polymerase Cell Biology Cold-shock domain Cold shock response Cold Temperature Cold Shock Proteins and Peptides Nucleic acid sense organs Molecular Chaperones Biotechnology |
| Zdroj: | Microbial Physiology. 17:110-117 |
| ISSN: | 2673-1673 2673-1665 |
| DOI: | 10.1159/000226587 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|