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.

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 Cold Shock Proteins of Lactococcus lactis MG1363 Are Involved in Cryoprotection and in the Production of Cold-Induced Proteins

2001 ◽  
Vol 67 (11) ◽  
pp. 5171-5178 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Hélène Frenkiel ◽  
Willem M. de Vos ◽  
Oscar P. Kuipers ◽  
Tjakko Abee
Keyword(s):  
Low Temperature ◽  
Lactococcus Lactis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Cold Shock ◽  
Transcriptional Level ◽  
Wild Type ◽  
Cold Shock Proteins ◽  
Shock Proteins ◽  
Induced Proteins

ABSTRACT Members of the group of 7-kDa cold-shock proteins (CSPs) are the proteins with the highest level of induction upon cold shock in the lactic acid bacterium Lactococcus lactis MG1363. By using double-crossover recombination, two L. lactis strains were generated in which genes encoding CSPs are disrupted: L. lactis NZ9000ΔAB lacks the tandemly orientatedcspA and cspB genes, and NZ9000ΔABE lackscspA, cspB, and cspE. Both strains showed no differences in growth at normal and at low temperatures compared to that of the wild-type strain, L. lactis NZ9000. Two-dimensional gel electrophoresis showed that upon disruption of thecspAB genes, the production of remaining CspE at low temperature increased, and upon disruption of cspA, cspB, and cspE, the production of CspD at normal growth temperatures increased. Northern blot analysis showed that control is most likely at the transcriptional level. Furthermore, it was established by a proteomics approach that some (non-7-kDa) cold-induced proteins (CIPs) are not cold induced in the csp-lacking strains, among others the histon-like protein HslA and the signal transduction protein LlrC. This supports earlier observations (J. A. Wouters, M. Mailhes, F. M. Rombouts, W. M. De Vos, O. P. Kuipers, and T. Abee, Appl. Environ. Microbiol. 66:3756–3763, 2000). that the CSPs of L. lactis might be directly involved in the production of some CIPs upon low-temperature exposure. Remarkably, the adaptive response to freezing by prior exposure to 10°C was significantly reduced in strain NZ9000ΔABE but not in strain NZ9000ΔAB compared to results with wild-type strain NZ9000, indicating a notable involvement of CspE in cryoprotection.

scholarly journals Selective mRNA Degradation by Polynucleotide Phosphorylase in Cold Shock Adaptation in Escherichia coli

2001 ◽  
Vol 183 (9) ◽  
pp. 2808-2816 ◽  
Author(s):  
Kunitoshi Yamanaka ◽  
Masayori Inouye
Keyword(s):  
Escherichia Coli ◽  
Cell Growth ◽  
Cold Shock ◽  
Critical Role ◽  
Rna Helicase ◽  
Cold Shock Protein ◽  
Polynucleotide Phosphorylase ◽  
Selective Degradation ◽  
High Level ◽  
Shock Proteins

ABSTRACT Upon cold shock, Escherichia coli cell growth transiently stops. During this acclimation phase, specific cold shock proteins (CSPs) are highly induced. At the end of the acclimation phase, their synthesis is reduced to new basal levels, while the non-cold shock protein synthesis is resumed, resulting in cell growth reinitiation. Here, we report that polynucleotide phosphorylase (PNPase) is required to repress CSP production at the end of the acclimation phase. A pnp mutant, upon cold shock, maintained a high level of CSPs even after 24 h. PNPase was found to be essential for selective degradation of CSP mRNAs at 15°C. In a poly(A) polymerase mutant and a CsdA RNA helicase mutant, CSP expression upon cold shock was significantly prolonged, indicating that PNPase in concert with poly(A) polymerase and CsdA RNA helicase plays a critical role in cold shock adaptation.

scholarly journals A Temperature-Independent Cold-Shock Protein Homolog Acts as a Virulence Factor in Xylella fastidiosa

2016 ◽  
Vol 29 (5) ◽  
pp. 335-344 ◽  
Author(s):  
Lindsey P. Burbank ◽  
Drake C. Stenger
Keyword(s):  
Deletion Mutant ◽  
Cold Shock ◽  
Rna Binding ◽  
Xylella Fastidiosa ◽  
Cold Shock Protein ◽  
Plant Colonization ◽  
Wild Type ◽  
Cold Temperatures ◽  
Mrna Stabilization

Xylella fastidiosa, causal agent of Pierce’s disease (PD) of grapevine, is a fastidious organism that requires very specific conditions for replication and plant colonization. Cold temperatures reduce growth and survival of X. fastidiosa both in vitro and in planta. However, little is known regarding physiological responses of X. fastidiosa to temperature changes. Cold-shock proteins (CSP), a family of nucleic acid–binding proteins, act as chaperones facilitating translation at low temperatures. Bacterial genomes often encode multiple CSP, some of which are strongly induced following exposure to cold. Additionally, CSP contribute to the general stress response through mRNA stabilization and posttranscriptional regulation. A putative CSP homolog (Csp1) with RNA-binding activity was identified in X. fastidiosa Stag’s Leap. The csp1 gene lacked the long 5′ untranslated region characteristic of cold-inducible genes and was expressed in a temperature-independent manner. As compared with the wild type, a deletion mutant of csp1 (∆csp1) had decreased survival rates following cold exposure and salt stress in vitro. The deletion mutant also was significantly less virulent in grapevine, as compared with the wild type, in the absence of cold stress. These results suggest an important function of X. fastidiosa Csp1 in response to cellular stress and during plant colonization.

scholarly journals Cold Shock Exoribonuclease R (VacB) Is Involved in Aeromonas hydrophila Pathogenesis

2008 ◽  
Vol 190 (10) ◽  
pp. 3467-3474 ◽  
Author(s):  
Tatiana E. Erova ◽  
Valeri G. Kosykh ◽  
Amin A. Fadl ◽  
Jian Sha ◽  
Amy J. Horneman ◽  
...  
Keyword(s):  
Low Temperature ◽  
Aeromonas Hydrophila ◽  
Cold Shock ◽  
Shigella Flexneri ◽  
Cold Shock Protein ◽  
Amino Acid Residues ◽  
Wild Type ◽  
Rnase R ◽  
Lethal Doses

ABSTRACT In this study, we cloned and sequenced a virulence-associated gene (vacB) from a clinical isolate SSU of Aeromonas hydrophila. We identified this gene based on our recently annotated genome sequence of the environmental isolate ATCC 7966T of A. hydrophila and the vacB gene of Shigella flexneri. The A. hydrophila VacB protein contained 798 amino acid residues, had a molecular mass of 90.5 kDa, and exhibited an exoribonuclease (RNase R) activity. The RNase R of A. hydrophila was a cold-shock protein and was required for bacterial growth at low temperature. The vacB isogenic mutant, which we developed by homologous recombination using marker exchange mutagenesis, was unable to grow at 4°C. In contrast, the wild-type (WT) A. hydrophila exhibited significant growth at this low temperature. Importantly, the vacB mutant was not defective in growth at 37°C. The vacB mutant also exhibited reduced motility, and these growth and motility phenotype defects were restored after complementation of the vacB mutant. The A. hydrophila RNase R-lacking strain was found to be less virulent in a mouse lethality model (70% survival) when given by the intraperitoneal route at as two 50% lethal doses (LD50). On the other hand, the WT and complemented strains of A. hydrophila caused 80 to 90% of the mice to succumb to infection at the same LD50 dose. Overall, this is the first report demonstrating the role of RNase R in modulating the expression of A. hydrophila virulence.

scholarly journals Role of Cold Shock Proteins in Growth of Listeria monocytogenes under Cold and Osmotic Stress Conditions

2009 ◽  
Vol 75 (6) ◽  
pp. 1621-1627 ◽  
Author(s):  
Barbara Schmid ◽  
Jochen Klumpp ◽  
Eveline Raimann ◽  
Martin J. Loessner ◽  
Roger Stephan ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Osmotic Stress ◽  
Cold Shock ◽  
Microbial Control ◽  
Nacl Stress ◽  
Stress Conditions ◽  
Control Measures ◽  
Cold Shock Protein ◽  
Osmotic Stress Tolerance ◽  
Shock Proteins

ABSTRACT The gram-positive bacterium Listeria monocytogenes is a food-borne pathogen of both public health and food safety significance. It possesses three small, highly homologous protein members of the cold shock protein (Csp) family. We used gene expression analysis and a set of mutants with single, double, and triple deletions of the csp genes to evaluate the roles of CspA, CspB, and CspD in the cold and osmotic (NaCl) stress adaptation responses of L. monocytogenes. All three Csps are dispensable for growth at optimal temperature (37°C). These proteins are, however, required for efficient cold and osmotic stress tolerance of this bacterium. The hierarchies of their functional importance differ, depending on the environmental stress conditions: CspA>CspD>CspB in response to cold stress versus CspD>CspA/CspB in response to NaCl salt osmotic stress. The fact that Csps are promoting L. monocytogenes adaptation against both cold and NaCl stress has significant implications in view of practical food microbial control measures. The combined or sequential exposure of L. monocytogenes cells to these two stresses in food environments might inadvertently induce cross-protection responses.

Construction of a [NiFe]-hydrogenase deletion mutant of Desulfovibrio vulgaris Hildenborough

2005 ◽  
Vol 33 (1) ◽  
pp. 59-60 ◽  
Author(s):  
A. Goenka ◽  
J.K. Voordouw ◽  
W. Lubitz ◽  
W. Gärtner ◽  
G. Voordouw
Keyword(s):  
Growth Phase ◽  
Exponential Growth ◽  
Deletion Mutant ◽  
Stationary Growth Phase ◽  
Exponential Growth Phase ◽  
Desulfovibrio Vulgaris ◽  
Wild Type ◽  
Stationary Growth ◽  
Desulfovibrio Vulgaris Hildenborough ◽  
Mutant Cells

A mutant of Desulfovibrio vulgaris Hildenborough lacking a gene for [NiFe] hydrogenase was generated. Growth studies, performed for the mutant in comparison with the wild-type, showed no strong differences during the exponential growth phase. However, the mutant cells died more rapidly in the stationary growth phase.

Expression of Major Cold Shock Proteins and Genes by Yersinia enterocolitica in Synthetic Medium and Foods

2005 ◽  
Vol 68 (11) ◽  
pp. 2454-2458 ◽  
Author(s):  
THIRUNAVUKKARASU ANNAMALAI ◽  
KUMAR VENKITANARAYANAN
Keyword(s):  
Yersinia Enterocolitica ◽  
Cold Shock ◽  
Synthetic Medium ◽  
Foodborne Pathogen ◽  
Skim Milk ◽  
Luria Bertani ◽  
Dot Blot ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Shock Proteins

Yersinia enterocolitica is a psychrotrophic foodborne pathogen that has been implicated in outbreaks of foodborne illness involving cold-stored foods, especially milk and pork. A major mechanism bacteria use to adapt to cold is expression of cold shock proteins. The objective of this research was to study the expression of major cold shock proteins of Y. enterocolitica in Luria-Bertani (LB) broth, milk, and pork following a temperature downshift from 30 to 4°C. Y. enterocolitica was inoculated into 10 ml of LB broth, sterile skim milk, or pork, and the samples were stored at 4°C (cold shock) or 30°C (control) for 0, 4, 8, 12, and 24 h. At each sampling time, total protein and total RNA were extracted from Y. enterocolitica harvested from LB broth, milk, and pork and subjected to two-dimensional gel electrophoresis and dot blot analysis. Two major cold shock proteins (CspA1 and CspA2) of ∼7 kDa and their genes were expressed by Y. enterocolitica following cold shock. However, the CspA1 and CspA2 proteins were not expressed by Y. enterocolitica at 30°C. Y. enterocolitica CspA1 and CspA2 were observed as early as 2 h of cold shock in cultures from LB broth and milk and at 8 h of cold shock in cultures from pork.

scholarly journals Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparum

2020 ◽  
Vol 19 (1) ◽  
Author(s):  
Ankita Behl ◽  
Vikash Kumar ◽  
Maxim Shevtsov ◽  
Shailja Singh
Keyword(s):  
Gene Expression ◽  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Cold Shock ◽  
Gene Expression Regulation ◽  
Protein Family ◽  
Cold Shock Protein ◽  
Parasite Life Cycle ◽  
Cold Shock Proteins ◽  
Shock Proteins

Abstract The cold shock domain (CSD) forms the hallmark of the cold shock protein family that provides the characteristic feature of binding with nucleic acids. While much of the information is available on bacterial, plants and human cold shock proteins, their existence and functions in the malaria parasite remains undefined. In the present review, the available information on functions of well-characterized cold shock protein members in different organisms has been collected and an attempt was made to identify the presence and role of cold shock proteins in malaria parasite. A single Plasmodium falciparum cold shock protein (PfCoSP) was found in P. falciparum which is reported to be essential for parasite survival. Essentiality of PfCoSP underscores its importance in malaria parasite life cycle. In silico tools were used to predict the features of PfCoSP and to identify its homologues in bacteria, plants, humans, and other Plasmodium species. Modelled structures of PfCoSP and its homologues in Plasmodium species were compared with human cold shock protein ‘YBOX-1’ (Y-box binding protein 1) that provide important insights into their functioning. PfCoSP model was subjected to docking with B-form DNA and RNA to reveal a number of residues crucial for their interaction. Transcriptome analysis and motifs identified in PfCoSP implicate its role in controlling gene expression at gametocyte, ookinete and asexual blood stages of malaria parasite. Overall, this review emphasizes the functional diversity of the cold shock protein family by discussing their known roles in gene expression regulation, cold acclimation, developmental processes like flowering transition, and flower and seed development, and probable function in gametocytogenesis in case of malaria parasite. This enables readers to view the cold shock protein family comprehensively.

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