Disease relevance of ECs4441

• The central nucleic acid binding domain of the vertebrate proteins is 43% identical to a 70-amino-acid-long protein (CS7.4) from E. coli [1].

High impact information on ECs4441

• Differential mRNA stability of the cspA gene in the cold-shock response of Escherichia coli [2].
• However, A9 was induced at high temperature by chloramphenicol, suggesting that CS7.4-like proteins have a more general role than their sole implication in cold acclimation processes [3].
• 4. The promoter of the gyrA gene contains specific binding sites for the CS7.4 protein, suggesting that CS7.4 acts at the transcriptional level to facilitate continued A-subunit synthesis [4].
• However, the differences in the nucleotide sequences between E. coli and S. enteritidis cspA genes in the putative repressor protein binding domain, the fragment 7, and in various segments throughout the upstream 0.642-kbp DNA may contribute to the expression of CS7.4 at less stringent temperatures in S. enteritidis [5].
• Parallel studies on CS7.4 and the Y-box proteins have elucidated both molecular mechanisms regulating the cold shock response and a novel site for the regulation of eukaryotic gene expression [6].

Biological context of ECs4441

• Our results suggest that mRNA stability plays a major role in the control of the cspA gene [2].

Analytical, diagnostic and therapeutic context of ECs4441

• A synthetic peptide was used to produce an antibody which detected a CS7.4-like protein (A9) by immunoblotting two-dimensional electrophoresis gels of A. globiformis SI55 total proteins [3].
• Western blot assay using E. coli CS7.4 antibody and analysis of radiolabeled total cellular proteins from S. typhimurium cultures after exposure to 10 degrees C or 5 degrees C showed elevated expression of a major cold shock protein, CS7 [7].

References