title: Unwinding activity of cold shock proteins and RNA metabolism.
abstract: Temperature downshift from 37 °C to 15 °C results in the exertion of cold shock response in Escherichia coli, which induces cold shock proteins, such as CsdA. Previously, we showed that the helicase activity of CsdA is critical for its function in the cold acclimation of cells and its primary role is mRNA degradation. Only RhlE (helicase), CspA (RNA chaperone) and RNase R (exoribonuclease) were found to complement the cold shock function of CsdA. RNase R has two independent activities, helicase and ribonuclease, only helicase being essential for the functional complementation of CsdA. Here, we discuss the significance of above findings as these emphasize the importance of the unwinding activity of cold-shock-inducible proteins in the RNA metabolism at low temperature, which may be different than that at 37 °C. It requires assistance of proteins to destabilize the secondary structures in mRNAs that are stabilized upon temperature downshift, hindering the activity of ribonucleases.
authors: Department of Biochemistry, Robert Wood Johnson Medical School, Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Piscataway, NJ, USA. phadtasa@umdnj.edu
authors: Sangita
authors: S
authors: Phadtare
mesh_terms: D057773:Cold Shock Proteins and Peptides / Q000378:metabolism*; D005095:Exoribonucleases / Q000378:metabolism; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D020365:RNA Helicases / Q000235:genetics / Q000378:metabolism; D013696:Temperature
chemical_list: D057773:Cold Shock Proteins and Peptides; D018832:Molecular Chaperones; D012313:RNA; D005095:Exoribonucleases; D020365:RNA Helicases