1995
DOI: 10.1111/j.1365-2958.1995.tb02431.x
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Mutational analysis of the putative nucleic acid‐binding surface of the cold‐shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single‐stranded DNA containing the Y‐box motif

Abstract: The major cold-shock protein of Bacillus subtilis, CspB, is a member of a protein family widespread among prokaryotes and eukaryotes that share the highly conserved cold-shock domain (CSD). The CSD domain is involved in transcriptional and translational regulation and was shown to bind the Y-box motif, a cis-element that contains the core sequence ATTGG, with high affinity. The three-dimensional structure of CspB, a prototype of this protein family, revealed that this hydrophilic CSD domain creates a surface r… Show more

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Cited by 138 publications
(172 citation statements)
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“…Several studies involving site-directed mutagenesis of aromatic patch residues have been performed. The results of these studies suggested that substitution of aromatic patch amino acids for leucine or serine residues destabilized Csp proteins and interfered with RNA binding (18,19). The results of these analyses extended our understanding of CspE structure and function but did not shed light into physiologically important nucleic acid melting function.…”
mentioning
confidence: 69%
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“…Several studies involving site-directed mutagenesis of aromatic patch residues have been performed. The results of these studies suggested that substitution of aromatic patch amino acids for leucine or serine residues destabilized Csp proteins and interfered with RNA binding (18,19). The results of these analyses extended our understanding of CspE structure and function but did not shed light into physiologically important nucleic acid melting function.…”
mentioning
confidence: 69%
“…We show that in addition to His 32 , Phe 17 and Phe 30 residues are also important for nucleic acid melting by CspE. On the other hand, substitutions of peripheral aromatic patch amino acid residues, Trp 10 , Phe 19 , and Phe 33 , have no effect on nucleic acid melting. Thus, the centrally located aromatic patch triad of Phe 17 , Phe 30 , and His 32 in CspE appears to initiate nucleic acid melting, which is then extended further to the periphery of the patch.…”
mentioning
confidence: 83%
“…CspA, the most prominent of the nine-member E. coli CSP family, accumulates up to 10% of total proteins during cold stress (Jiang et al, 1997). The three-dimensional structure of E. coli CspA forms a five-stranded ␤-barrel structure (Newkirk et al, 1994;Schindelin et al, 1994) that contains two consensus RNA-binding motifs (RNP1 and RNP2), which facilitate nucleic acid recognition/binding (Schroder et al, 1995). CspA has been hypothesized to prevent RNA secondary structure formation (Jiang et al, 1997), thereby enhancing translation at low temperature.…”
mentioning
confidence: 99%
“…CSPs possess binding sites for singlestranded nucleic acids on their antiparallel three-stranded ␤-sheets, which involve basic and aromatic residues. These are the so-called RNA-binding ribonucleoprotein motifs (13,14).CSPs were discovered originally because they are strongly induced in response to cold shock (15), and thus they were assumed to be important for adaptation to low temperatures. The major cold shock protein, CspA from E. coli, was in fact shown to increase the synthesis of several cold stress-inducible proteins after a decrease in temperature (16).…”
mentioning
confidence: 99%
“…CSPs possess binding sites for singlestranded nucleic acids on their antiparallel three-stranded ␤-sheets, which involve basic and aromatic residues. These are the so-called RNA-binding ribonucleoprotein motifs (13,14).…”
mentioning
confidence: 99%