Disease relevance of cspA

• Acquirement of cold sensitivity by quadruple deletion of the cspA family and its suppression by PNPase S1 domain in Escherichia coli [1].
• Cloning of two cold shock genes, cspA and cspG, from the deep-sea psychrophilic bacterium Shewanella violacea strain DSS12 [2].
• Identification and characterization of five cspA homologous genes from Myxococcus xanthus [3].
• The three-dimensional structure of CspA is similar to that of the major cold shock protein of Bacillus subtilis, CspB, which has recently been determined at 2.45-A resolution [4].
• Acclimatization of the psychrotolerant Yersinia enterocolitica after a cold shock from 30 degrees C to 10 degrees C causes transcription of the major cold shock protein (CSP) bicistronic gene cspA1/A2 to increase by up to 300-fold [5].

High impact information on cspA

• The cspA mRNA level decreases rapidly with increasing cell density, becoming virtually undetectable by mid-to-late exponential growth phase while the CspA level declines, although always remaining clearly detectable [6].
• The cspA mRNA instability is due to its 5' untranslated leader and is counteracted in vivo by the cold-shock DeaD box RNA helicase (CsdA) [6].
• This induction required the varsigma factor, RpoS, but was independent of the major cold-shock protein, CspA. otsA/B mRNA was much more stable at 16 degrees C than at 37 degrees C and contained a "downstream box," characteristic of cold-inducible mRNAs [7].
• The relaxation kinetics of the major cold shock protein of Escherichia coli (CspA) in response to a laser-induced temperature jump are exponential for small temperature jumps, indicative of folding through a two-state mechanism [8].
• Our results demonstrate that the AUG initiation codon and the coding region containing the downstream box are not required for cspA mRNA to bind ribosomes and that the 5'-untranslated region by itself has a remarkable affinity to ribosomes at low temperature [9].

Chemical compound and disease context of cspA

• Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene [10].
• Global effects of homocysteine on transcription in Escherichia coli: induction of the gene for the major cold-shock protein, CspA [11].

Biological context of cspA

• Based on these results, we suggest that the role of the CSC-box is related to downregulation of cspA mRNA after acclimation to low temperature [5].
• Screening for mutations among common laboratory E. coli strains showed a high degree of genetic diversity in cspC but not in cspA and cspE [12].
• The amount of mRNA from the chromosomal cspA gene was much higher in cells overproducing the wild-type 5' UTR by means of a plasmid than it was in cells overproducing the cold-box-deleted 5' UTR [13].
• Identification of the promoter region of the Escherichia coli major cold shock gene, cspA [14].
• The role of the cold-box region was further confirmed with a cspA mutant strain containing a cold-box-deleted cspA gene integrated into the chromosome, which showed a high level of constitutive production of CspA but not CspB during exponential growth at low temperature [13].

Anatomical context of cspA

• We demonstrate that the observed growth inhibition was caused by largely exclusive occupation of cellular ribosomes by the mutant cspA mRNAs [15].

Associations of cspA with chemical compounds

• Aspergillus niger NW156 prtF pyrA leuA cspA transformed with the pyrA containing plasmid and a plasmid harboring the complete vaoA gene including the promoter and terminator was able to produce vaoA mRNA and active vanillyl-alcohol oxidase when grown on veratryl alcohol and anisyl alcohol [16].
• Finally, in contrast to a previous claim, translation of cold-shock cspA mRNA in the cold was found to be as sensitive as that of a non-cold-shock mRNA to both chloramphenicol and kanamycin inhibition [17].
• The induction of cspA by Hcy was suppressed when isoleucine was included in the growth medium [11].
• Conservation of the major cold shock protein in lactic acid bacteria [18].

Other interactions of cspA

• Surprisingly, E. coli contains a large CspA family, consisting of nine genes from cspA to cspI [19].
• Characterization of cspB, a cold-shock-inducible gene from Lactococcus lactis, and evidence for a family of genes homologous to the Escherichia coli cspA major cold shock gene [20].
• The performance of the major Escherichia coli cold-shock promoter in directing the synthesis of recombinant proteins at low temperatures was investigated in batch fermentations using a plasmid-encoded transcriptional gene fusion between the cspA promoter region and the lacZ gene [21].
• It has been proposed that this effect is due to highly conserved 11-base sequences designated the "cold box" existing in the 5' UTRs of cspA, cspB, and csdA [13].
• Inactivation of fecR results in significant increases in both cell aggregation and biofilm formation, while the effects of cspA are not as strong in the conditions tested [22].

Analytical, diagnostic and therapeutic context of cspA

• Detection and speciation of bacteria through PCR using universal major cold-shock protein primer oligomers [23].
• Expression of the cspA gene in Escherichia coli led to the production of a major anti-CspA-labeled protein of 80,000 Da which was purified by affinity chromatography on DEAE-cellulose [10].
• RT-PCR and reporter fusion experiments confirmed that cspA was induced by Hcy [11].
• Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB [24].
• CS7.4 is the major cold-shock protein specifically expressed to a level as high as 13% of the total cellular protein within the first hour when Escherichia coli cell culture is shifted from 37 to 15 degrees C [Goldstein et al. (1990) Proc. Natl. Acad. Sci. USA 87, 283-287] [25].

References