CspA, the major cold-shock protein of Escherichia coli, is dramatically induced during the
cold-shock response. The amino acid sequence of CspA shows 43% identity to the" cold …

Ensuring the correct folding of RNA molecules in the cell is of major importance for a large
variety of biological functions. Therefore, chaperone proteins that assist RNA in adopting …

One of the many important consequences that temperature down-shift has on cells is
stabilization of secondary structures of RNAs. This stabilization has wide-spread effects …

CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone, which is
thought to facilitate translation at low temperature by destabilizing mRNA structures. Here …

CspA was originally found as the major cold‐shock protein in Escherichia coli, consisting of
70‐amino‐acid residues. It forms a β‐barrel structure with five anti‐parallel β‐strands and …

Cold induction of cspA, the paradigm Escherichia coli cold-shock gene, is mainly subject to
posttranscriptional control, partly promoted by cis-acting elements of its transcript, whose …

When the gene for CspA, the major cold shock protein of Escherichia coli, was disrupted by
a novel positive/negative selection method, the deltacspA cells did not show any discernible …

The gene for CspA, the major cold‐shock protein of Escherichia coli is known to be
dramatically induced upon temperature downshift. Here, we report that three‐base …

Members of a family of cold-shock proteins (CSPs) are found throughout the eubacterial
domain and appear to function as RNA-chaperones. They have been implicated in various …

Upon temperature downshift, a group of proteins called cold shock proteins, such as CspA,
CspB, and CsdA, are transiently induced in Escherichia coli. However, when the 5 …