Structure and function of bacterial cold shock proteins

  title={Structure and function of bacterial cold shock proteins},
  author={Gudrun Horn and Roland Hofweber and Werner Kremer and Hans Robert Kalbitzer},
  journal={Cellular and Molecular Life Sciences},
Abstract.Cold shock proteins (Csps) comprise a family of small proteins that are structurally highly conserved and bind to single-stranded nucleic acids via their nucleic acid binding motifs RNP1 and RNP2. Bacterial Csps are mainly induced after a rapid temperature downshift to regulate the adaptation to cold stress, but are also present under normal conditions to regulate other biological functions. The structural unit characteristic for Csps occurs also as a cold shock domain (CSD) in other… 

Eukaryotic cold shock domain proteins: highly versatile regulators of gene expression

This review summarizes the current knowledge on eukaryotic CSD/S1 domain‐containing proteins with a special emphasis on UNR (upstream of N‐ras), a member of this family with multiple copies of the CSD.

Dynamical properties of cold shock protein A from Mycobacterium tuberculosis.

Cold Shock Domain Proteins: Structure and Interaction with Nucleic Acids

This review describes similarities and differences in the structure of cold shock proteins of prokaryotes and CSD proteins of eukaryotes with special emphasis on the functions related to the RNA/DNA-binding ability of these proteins.

Isolation of Two Strong Poly (U) Binding Proteins from Moderate Halophile Halomonas eurihalina and Their Identification as Cold Shock Proteins

Two strong poly (U) binding proteins in abundance are observed in abundance in cell extracts from cells grown under normal growth conditions and identified as major cold shock proteins belonging to Csp A family by MALDI-TOF and bioinformatic analysis.

Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium.

The crystal structure of cold-shock protein E from S. typhimurium (StCspE) has been determined and is similar to those of previously determined CSPs and is composed of five antiparallel beta-strands forming a classic OB fold/five-stranded beta-barrel.

Sequence, structure and evolutionary analysis of cold shock domain proteins, a member of OB fold family

Analysis of sequence distribution suggesting that CSDs are largely found in bacteria (83–94%) with single CSD repeat, and analysis of repeats distributions on evolutionary scale suggest that existence of CSD in multiple repeats is mainly driven through speciation, gene shuffling and gene duplication events.

Conserved TRAM Domain Functions as an Archaeal Cold Shock Protein via RNA Chaperone Activity

Physiological and biochemical studies on four TRAM proteins from a cold adaptive archaeon Methanolobus psychrophilus R15 demonstrated that TRAM is an archaeal Csp and exhibits RNA chaperone activity, validating the RNA chacherone activity of TRAMs.

shock protein in crystals and solution RNA single strands bind to a conserved surface of the major cold

Bacterial cold shock proteins (CSPs) regulate the cellular response to temperature downshift through RNA chaperoning and transcriptional antitermination and binding studies demonstrate that Bs-CspB associates with ssDNA as well as ssRNA with moderate sequence specificity.

Contribution of Eutrema salsugineum Cold Shock Domain Structure to the Interaction with RNA

Three recombinant CSDPs from the saltwater cress plant were used and it was shown that their nonspecific interaction with RNA is determined by their C-terminal fragments, and all three proteins exhibited high affinity to the single-stranded regions over four nucleotides long within RNA oligonucleotides.

Bacterial Cold Shock Proteins - the Molecular Chaperones for Multiple Stress Tolerance

The Csps are one of the major Cips produced under cold conditions mainly in bacteria and help to resolve the misfolded RNA structures under abiotic stress conditions.



Bacterial cold-shock proteins

A number of experimental evidences suggests that CSPs bind messenger RNA (mRNA) and regulate ribosomal translation, rate of mRNA degradation and termination of transcription in cold-shock adaptation.

Crystal structure of CspA, the major cold shock protein of Escherichia coli.

Due to the high homology of the bacterial cold shock proteins with the Y-box factors, E. coli CspA and B. subtilis CspB define a structural framework for the common cold shock domain.

CspA, the Major Cold-shock Protein of Escherichia coli, Is an RNA Chaperone*

It is proposed that CspA functions as an RNA chaperone to prevent the formation of secondary structures in RNA molecules at low temperature and may be crucial for efficient translation of mRNAs at low temperatures and may also have an effect on transcription.

Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein

As a prototype of the cold-shock domain, the structure of CspB has been determined here from two crystal forms and is present as an antiparallel five-stranded β-barrel that is presumably involved in nucleic acid binding.

Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.

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Structure in solution of the major cold-shock protein from Bacillus subtilis

The three-dimensional structure of CspB, the major cold-shock proteins of Escherichia coli and B. subtilis, is determined by nuclear magnetic resonance spectroscopy and resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein.

The influence of cold shock proteins on transcription and translation studied in cell‐free model systems

A concentration‐dependent suppression of transcription and translation by the different CSPs is observed which makes the considered addition of C SPs for enhancing the protein expression in in’vitro translation systems obsolete.