Accumulation of proteins of the cold shock domain (CSD) family and the regulation of their corresponding genes is one of the adaptive Dabrafenib price responses to
cold temperatures that has been described in both mesophilic and psychrotolerant bacteria including Escherichia coli (Phadtare et al., 1999), Bacillus subtilis (Schindler et al., 1999), Arthrobacter globiformis (Berger et al., 1996), Pseudomonas putida (Gumley & Inniss, 1996), Salmonella spp. (Jeffreys et al., 1998), Rhodococcus spp.(Bej et al., 2000) and Pseudomonas sp.30-3 (Panicker et al., 2002). The CSD has been reported to be an evolutionarily conserved nucleic acid-binding domain of ancient origin found in eubacteria. It is also homologous to the CSD in human Y-box protein YB-1 and to other eukaryotic Y-box proteins (Graumann & Marahiel, 1998). The structures of cold-shock proteins (Csps) from different bacteria have been determined by either X-ray crystallography or nuclear magnetic resonance, for example E. coli CspA (Newkirk et al., 1994; Schindelin et al., 1994), B. subtilis
CspB (Schnuchel et al., 1993), Bacillus caldolyticus Csp (Mueller et al., 2000), Thermotoga maritima Csp (Kremer et al., 2001) and Neisseria meningitidis Csp (Ren et al., 2008). All of them share a common OB (oligonucleotide/oligosaccharide-binding) see more fold consisting of five β-barrel sheets with two consensus RNA-binding domains (RNP1 and RNP2) placed side by side on separate β-sheets, comprising a high proportion of basic and aromatic residues. The binding of B. subtilis CspB and B. caldolyticus Csp with hexathymidine (dT6) involves stacking interactions between phenylalanine residues and the thymidine base, together with hydrogen bonds between the side chains of polar amino acids and pyrimidine
bases (Max et al., 2007). Escherichia coli CspA family of proteins consist of nine homologs to the major cold-shock protein CspA (CS7.4) (Phadtare et al., 1999) and they either function as a RNA chaperones by minimizing the secondary structure formation in mRNAs to allow efficient translation at low temperatures or as transcription regulators and transcription antiterminators (Bae et al., 2000). Escherichia coli CspA, CspB, CspG and CspI are cold inducible, whereas CspC and CspE are constitutively expressed Inositol oxygenase and have been shown to function as suppressors of the temperature-sensitive mukB106 mutation. The mukB gene is involved in the chromosome partitioning during cell division in E. coli (Yamanaka et al., 1994). The expression of E. coli cspF and cspH has not been associated with any particular growth condition or phenotype (Giaquinto et al., 2007). Non-cold-inducible E. coli CspD functions as a DNA replication inhibitor during the stationary growth phase. Its expression is inversely dependent upon the growth rate and induced upon glucose starvation at 37 °C (Yamanaka & Inouye, 1997).