Bacterial cold-shock proteins

No abstract is available for this paper.

• Publication year

  2002

• Venue

  Cellular and Molecular Life Sciences (CMLS)

• Publication date

  2002-11-01

• Fields of study

  Biology, Medicine, Environmental Science

• Identifiers
  DOI 10.1007/PL00012513PMID 12530521PMCID PMC11337450
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1.

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• The Cold Box Stem-loop Proximal to the 5′-End of theEscherichia coli cspA Gene Stabilizes Its mRNA at Low Temperature*

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• Different in vivo localization of the Escherichia coli proteins CspD and CspA.

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• Complementation of Cold Shock Proteins by Translation Initiation Factor IF1 In Vivo

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• Translation during cold adaptation does not involve mRNA-rRNA base pairing through the downstream box.

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• Interactions of the Major Cold Shock Protein of Bacillus subtilis CspB with Single-stranded DNA Templates of Different Base Composition*

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• CspA, CspB, and CspG, Major Cold Shock Proteins ofEscherichia coli, Are Induced at Low Temperature under Conditions That Completely Block Protein Synthesis

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• Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis

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• Translational regulation by Y-box transcription factor: involvement of the major mRNA-associated protein, p50.

  1999cited by this paper
• Transcription of cspA, the gene for the major cold-shock protein of Escherichia coli, is negatively regulated at 37 degrees C by the 5'-untranslated region of its mRNA.

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• Expression of the Csp protein family upon cold shock and production of tetracycline in Streptomyces aureofaciens.

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  1998cited by this paper
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• Role of the Cold-Box Region in the 5′ Untranslated Region of the cspA mRNA in Its Transient Expression at Low Temperature in Escherichia coli

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