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Cold-shock domain

Protein domain


Summary

Protein domain

FieldValue
SymbolCSD
NameCSD
imagePDB 1h95 EBI.jpg
captionsolution structure of the single-stranded dna-binding cold shock domain (csd) of human y-box protein 1 (yb1) determined by nmr (10 lowest energy structures)
PfamPF00313
Pfam_clanCL0021
InterProIPR002059
PROSITEPDOC00304
SCOP1mjc
CDDcd04458

In molecular biology, the cold-shock domain (CSD) is a protein domain of about 70 amino acids which has been found in prokaryotic and eukaryotic DNA-binding proteins. Part of this domain is highly similar to the RNP-1 RNA-binding motif.

When Escherichia coli is exposed to a temperature drop from 37 to 10 degrees Celsius, a 4–5 hour lag phase occurs, after which growth is resumed at a reduced rate. During the lag phase, the expression of around 13 proteins, which contain cold shock domains is increased 2–10 fold. These so-called cold shock proteins induced in the cold shock response are thought to help the cell to survive in temperatures lower than optimum growth temperature, by contrast with heat shock proteins induced in the heat shock response, which help the cell to survive in temperatures greater than the optimum, possibly by condensation of the chromosome and organisation of the prokaryotic nucleoid.

References

References

  1. (April 1992). "The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif". New Biol..
  2. Wistow G. (April 1990). "Cold shock and DNA binding". Nature.
  3. (March 1994). "The cold-shock response--a hot topic". Mol. Microbiol..
  4. Landsman D. (June 1992). "RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain". Nucleic Acids Res..
  5. (October 1991). "Nucleotide sequence of a cDNA clone encoding a putative glycine-rich protein of 19.7 kDa in Nicotiana sylvestris". Plant Mol. Biol..
  6. (November 1990). "Xenopus Y-box transcription factors: molecular cloning, functional analysis and developmental regulation". Proc. Natl. Acad. Sci. U.S.A..
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