Electrostatic stabilization of a thermophilic cold shock protein

2002 ◽  
Vol 316 (1) ◽  
pp. 213 ◽  
Author(s):  
D. Perl ◽  
F.X. Schmid
Keyword(s):  
Cold Shock ◽  
Cold Shock Protein ◽  
Electrostatic Stabilization

Study on the transgenic tobacco expressing truncated wheat cold shock protein gene TA3-13 and analysis of disease resistance

2011 ◽  
Vol 33 (5) ◽  
pp. 520-526 ◽  
Author(s):  
Na LI ◽  
Xiu-Zhen DU ◽  
Xiao-Mei PAN ◽  
Jin-Sheng WANG ◽  
Cong-Feng SONG
Keyword(s):  
Disease Resistance ◽  
Transgenic Tobacco ◽  
Cold Shock ◽  
Protein Gene ◽  
Cold Shock Protein

Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis

2015 ◽  
Vol 112 ◽  
pp. 15-20 ◽  
Author(s):  
Antje Lindae ◽  
Raphael J. Eberle ◽  
Icaro P. Caruso ◽  
Monika A. Coronado ◽  
Fabio R. de Moraes ◽  
...  
Keyword(s):  
Cold Shock ◽  
Protein A ◽  
Cold Shock Protein ◽  
Corynebacterium Pseudotuberculosis ◽  
Purification And Characterization

Dynamical properties of cold shock protein A from Mycobacterium tuberculosis

2010 ◽  
Vol 402 (4) ◽  
pp. 693-698 ◽  
Author(s):  
Gabriella D’Auria ◽  
Carla Esposito ◽  
Lucia Falcigno ◽  
Luisa Calvanese ◽  
Emanuela Iaccarino ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cold Shock ◽  
Protein A ◽  
Cold Shock Protein ◽  
Dynamical Properties

scholarly journals Major cold shock protein of Escherichia coli.

1990 ◽  
Vol 87 (1) ◽  
pp. 283-287 ◽  
Author(s):  
J. Goldstein ◽  
N. S. Pollitt ◽  
M. Inouye
Keyword(s):  
Escherichia Coli ◽  
Cold Shock ◽  
Cold Shock Protein

scholarly journals Metabolomic Evaluation of Ralstonia solanacearum Cold Shock Protein Peptide (csp22)-Induced Responses in Solanum lycopersicum

2022 ◽  
Vol 12 ◽  
Author(s):  
Dylan R. Zeiss ◽  
Paul A. Steenkamp ◽  
Lizelle A. Piater ◽  
Ian A. Dubery
Keyword(s):  
Solanum Lycopersicum ◽  
Bacterial Wilt ◽  
Ralstonia Solanacearum ◽  
Plant Pathogens ◽  
Cold Shock ◽  
Phenylpropanoid Pathway ◽  
Infection Process ◽  
Cold Shock Protein ◽  
Pre Treatment ◽  
Molecular Patterns

Ralstonia solanacearum, the causal agent of bacterial wilt, is one of the most destructive bacterial plant pathogens. This is linked to its evolutionary adaptation to evade host surveillance during the infection process since many of the pathogen’s associated molecular patterns escape recognition. However, a 22-amino acid sequence of R. solanacearum-derived cold shock protein (csp22) was discovered to elicit an immune response in the Solanaceae. Using untargeted metabolomics, the effects of csp22-elicitation on the metabolome of Solanum lycopersicum leaves were investigated. Additionally, the study set out to discover trends that may suggest that csp22 inoculation bestows enhanced resistance on tomato against bacterial wilt. Results revealed the redirection of metabolism toward the phenylpropanoid pathway and sub-branches thereof. Compared to the host response with live bacteria, csp22 induced a subset of the discriminant metabolites, but also metabolites not induced in response to R. solanacearum. Here, a spectrum of hydroxycinnamic acids (especially ferulic acid), their conjugates and derivatives predominated as signatory biomarkers. From a metabolomics perspective, the results support claims that csp22 pre-treatment of tomato plants elicits increased resistance to R. solanacearum infection and contribute to knowledge on plant immune systems operation at an integrative level. The functional significance of these specialized compounds may thus support a heightened state of defense that can be applied to ward off attacking pathogens or toward priming of defense against future infections.

scholarly journals Localization of Cold Shock Proteins to Cytosolic Spaces Surrounding Nucleoids in Bacillus subtilis Depends on Active Transcription

2001 ◽  
Vol 183 (21) ◽  
pp. 6435-6443 ◽  
Author(s):  
Michael H. W. Weber ◽  
Arsen V. Volkov ◽  
Ingo Fricke ◽  
Mohamed A. Marahiel ◽  
Peter L. Graumann
Keyword(s):  
Bacillus Subtilis ◽  
Cold Shock ◽  
Fluorescent Protein ◽  
Cold Shock Protein ◽  
Initiation Of Translation ◽  
Specific Localization ◽  
Active Transcription ◽  
Green Fluorescent ◽  
Shock Proteins ◽  
Mutant Cells

ABSTRACT Using immunofluorescence microscopy and a fusion of a cold shock protein (CSP), CspB, to green fluorescent protein (GFP), we showed that in growing cells Bacillus subtilis CSPs specifically localize to cytosolic regions surrounding the nucleoid. The subcellular localization of CSPs is influenced by the structure of the nucleoid. Decondensed chromosomes in smc mutant cells reduced the sizes of the regions in which CSPs localized, while cold shock-induced chromosome compaction was accompanied by an expansion of the space in which CSPs were present. As a control, histone-like protein HBsu localized to the nucleoids, while β-galactosidase and GFP were detectable throughout the cell. After inhibition of translation, CspB-GFP was still present around the nucleoids in a manner similar to that in cold-shocked cells. However, in stationary-phase cells and after inhibition of transcription, CspB was distributed throughout the cell, indicating that specific localization of CspB depends on active transcription and is not due to simple exclusion from the nucleoid. Furthermore, we observed that nucleoids are more condensed and frequently abnormal incspB cspC and cspB cspDdouble-mutant cells. This suggests that the function of CSPs affects chromosome structure, probably through coupling of transcription to translation, which is thought to decondense nucleoids. In addition, we found that cspB cspD and cspB cspC double mutants are defective in sporulation, with a block at or before stage 0. Interestingly, CspB and CspC are depleted from the forespore compartment but not from the mother cell. In toto, our findings suggest that CSPs localize to zones of newly synthesized RNA, coupling transcription with initiation of translation.

scholarly journals Autoantibody Formation and Mapping of Immunogenic Epitopes against Cold-Shock-Protein YB-1 in Cancer Patients and Healthy Controls

Cancers ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 3507
Author(s):  
Ronnie Morgenroth ◽  
Charlotte Reichardt ◽  
Johannes Steffen ◽  
Stefan Busse ◽  
Ronald Frank ◽  
...  
Keyword(s):  
Cancer Patients ◽  
Cold Shock ◽  
Full Length ◽  
Cold Shock Protein ◽  
Autoimmune Response ◽  
Healthy Controls ◽  
Protein Cleavage ◽  
Systematic Analysis ◽  
Linear Epitopes ◽  
Autoantibody Formation

Cold shock Y-box binding protein-1 participates in cancer cell transformation and mediates invasive cell growth. It is unknown whether an autoimmune response against cancerous human YB-1 with posttranslational protein modifications or processing develops. We performed a systematic analysis for autoantibody formation directed against conformational and linear epitopes within the protein. Full-length and truncated recombinant proteins from prokaryotic and eukaryotic cells were generated. Characterization revealed a pattern of spontaneous protein cleavage, predominantly with the prokaryotic protein. Autoantibodies against prokaryotic, but not eukaryotic full-length and cleaved human YB-1 protein fragments were detected in both, healthy volunteers and cancer patients. A mapping of immunogenic epitopes performed with truncated E. coli-derived GST-hYB-1 proteins yielded distinct residues in the protein N- and C-terminus. A peptide array with consecutive overlapping 15mers revealed six distinct antigenic regions in cancer patients, however to a lesser extent in healthy controls. Finally, a protein cleavage assay was set up with recombinant pro- and eukaryotic-derived tagged hYB-1 proteins. A distinct cleavage pattern developed, that is retarded by sera from cancer patients. Taken together, a specific autoimmune response against hYB-1 protein develops in cancer patients with autoantibodies targeting linear epitopes.

scholarly journals Restart of Exponential Growth of Cold-Shocked Yersinia enterocolitica Occurs after Down-Regulation ofcspA1/A2 mRNA

2000 ◽  
Vol 182 (11) ◽  
pp. 3285-3288 ◽  
Author(s):  
Klaus Neuhaus ◽  
Sonja Rapposch ◽  
Kevin P. Francis ◽  
Siegfried Scherer
Keyword(s):  
Yersinia Enterocolitica ◽  
Exponential Growth ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Clear Correlation ◽  
Wild Type ◽  
Tandem Gene Duplication ◽  
Cellular Content ◽  
Shock Proteins ◽  
Mutant Cells

ABSTRACT The cellular content of major cold shock protein (MCSP) mRNA transcribed from the tandem gene duplication cspA1/A2 and growth of Yersinia enterocolitica were compared when exponentially growing cultures of this bacterium were cold shocked from 30 to 20, 15, 10, 5, or 0°C, respectively. A clear correlation between the time point when exponential growth resumes after cold shock and the degradation of cspA1/A2 mRNA was found. A polynucleotide phosphorylase-deficient mutant was unable to degradecspA1/A2 mRNA properly and showed a delay, as well as a lower rate, of growth after cold shock. For this mutant, a correlation between decreasing cspA1/A2 mRNA and restart of growth after cold shock was also observed. For both wild-type and mutant cells, no correlation of restart of growth with the cellular content of MCSPs was found. We suggest that, after synthesis of cold shock proteins and cold adaptation of the cells, MCSP mRNAs must be degraded; otherwise, they trap ribosomes, prevent translation of bulk mRNA, and thus inhibit growth of this bacterium at low temperatures.

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