scholarly journals Identification and Transcriptional Control of Caulobacter crescentus Genes Encoding Proteins Containing a Cold Shock Domain

2004 ◽  
Vol 186 (17) ◽  
pp. 5603-5613 ◽  
Author(s):  
Elza A. S. Lang ◽  
Marilis V. Marques
Keyword(s):  
Transcriptional Control ◽  
Cold Shock ◽  
Caulobacter Crescentus ◽  
Transcriptional Level ◽  
Deletion Mapping ◽  
Nucleic Acid Binding ◽  
Cold Shock Proteins ◽  
Reverse Transcription Pcr ◽  
Cold Shock Domain ◽  
Shock Proteins

ABSTRACT The cold shock proteins are small peptides that share a conserved domain, called the cold shock domain (CSD), that is important for nucleic acid binding. The Caulobacter crescentus genome has four csp genes that encode proteins containing CSDs. Three of these (cspA, cspB, and cspC) encode peptides of about 7 kDa and are very similar to the cold shock proteins of other bacteria. Analysis by reverse transcription-PCR of the fourth gene (cspD), which was previously annotated as encoding a 7-kDa protein, revealed that the mRNA is larger and probably encodes a putative 21-kDa protein, containing two CSDs. A search in protein sequences databases revealed that this new domain arrangement has thus far only been found among deduced peptides of α-proteobacteria. Expression of each Caulobacter csp gene was studied both in response to cold shock and to growth phase, and we have found that only cspA and cspB are induced by cold shock, whereas cspC and cspD are induced at stationary phase, with different induction rates. The transcription start sites were determined for each gene, and a deletion mapping of the cspD promoter region defined a sequence required for maximal levels of expression, indicating that regulation of this gene occurs at the transcriptional level. Deletion of cspA, but not cspD, caused a reduction in viability when cells were incubated at 10°C for prolonged times, suggesting that cspA is important for adaptation to a low temperature.

scholarly journals Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding

Cancers ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 190
Author(s):  
Udo Heinemann ◽  
Yvette Roske
Keyword(s):  
Cold Shock ◽  
Rna Binding ◽  
Binding Mode ◽  
Nucleic Acid Binding ◽  
Cold Shock Proteins ◽  
Dna And Rna ◽  
Promiscuous Dna ◽  
Human Proteins ◽  
Cold Shock Domain ◽  
Shock Proteins

The cold-shock domain has a deceptively simple architecture but supports a complex biology. It is conserved from bacteria to man and has representatives in all kingdoms of life. Bacterial cold-shock proteins consist of a single cold-shock domain and some, but not all are induced by cold shock. Cold-shock domains in human proteins are often associated with natively unfolded protein segments and more rarely with other folded domains. Cold-shock proteins and domains share a five-stranded all-antiparallel β-barrel structure and a conserved surface that binds single-stranded nucleic acids, predominantly by stacking interactions between nucleobases and aromatic protein sidechains. This conserved binding mode explains the cold-shock domains’ ability to associate with both DNA and RNA strands and their limited sequence selectivity. The promiscuous DNA and RNA binding provides a rationale for the ability of cold-shock domain-containing proteins to function in transcription regulation and DNA-damage repair as well as in regulating splicing, translation, mRNA stability and RNA sequestration.

scholarly journals Cold Shock GenescspAandcspBfrom Caulobacter crescentus Are Posttranscriptionally Regulated and Important for Cold Adaptation

2012 ◽  
Vol 194 (23) ◽  
pp. 6507-6517 ◽  
Author(s):  
Ricardo R. Mazzon ◽  
Elza A. S. Lang ◽  
Carolina A. P. T. Silva ◽  
Marilis V. Marques
Keyword(s):  
Cold Adaptation ◽  
Cold Shock ◽  
Caulobacter Crescentus ◽  
Deletion Mapping ◽  
Nucleic Acid Binding ◽  
Content Type ◽  
Mrna Stabilization ◽  
Temperature Downshift ◽  
Shock Proteins ◽  
Cold Induction

ABSTRACTCold shock proteins (CSPs) are nucleic acid binding chaperones, first described as being induced to solve the problem of mRNA stabilization after temperature downshift.Caulobacter crescentushas four CSPs: CspA and CspB, which are cold induced, and CspC and CspD, which are induced only in stationary phase. In this work we have determined that the synthesis of both CspA and CspB reaches the maximum levels early in the acclimation phase. The deletion ofcspAcauses a decrease in growth at low temperature, whereas the strain with a deletion ofcspBhas a very subtle and transient cold-related growth phenotype. ThecspA cspBdouble mutant has a slightly more severe phenotype than that of thecspAmutant, suggesting that although CspA may be more important to cold adaptation than CspB, both proteins have a role in this process. Gene expression analyses were carried out usingcspAandcspBregulatory fusions to thelacZreporter gene and showed that both genes are regulated at the transcriptional and posttranscriptional levels. Deletion mapping of the long 5′-untranslated region (5′-UTR) of each gene identified a common region important for cold induction, probably via translation enhancement. In contrast to what was reported for other bacteria, these cold shock genes have no regulatory regions downstream from ATG that are important for cold induction. This work shows that the importance of CspA and CspB toC. crescentuscold adaptation, mechanisms of regulation, and pattern of expression during the acclimation phase apparently differs in many aspects from what has been described so far for other bacteria.

scholarly journals Predicted Cold Shock Proteins from the Extremophilic Bacterium Deinococcus maricopensis and Related Deinococcus Species

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Michael J. LaGier
Keyword(s):  
Cold Shock ◽  
Temperature Adaptation ◽  
Nucleic Acid Binding ◽  
Binding Motifs ◽  
Cold Shock Proteins ◽  
Cold Environments ◽  
Cold Shock Domain ◽  
Bioinformatic Approaches ◽  
Shock Proteins ◽  
Genome Information

While many studies have examined the mechanisms by which extremophilic Deinococci survive exposure to ionizing radiation, very few publications have characterized the cold shock adaptations of this group, despite many species being found in persistent cold environments and environments prone to significant daily temperature fluctuations. Bacterial cold shock proteins (Csps) are a family of conserved, RNA chaperone proteins that commonly play a role in cold temperature adaptation, including a downward shift in temperature (i.e., cold shock). The primary aim of this study was to test whether a representative, desert-dwelling Deinococcus, Deinococcus maricopensis, encodes Csps as part of its genome. Bioinformatic approaches were used to identify a Csp from D. maricopensis LB-34. The Csp, termed Dm-Csp1, contains sequence features of Csps including a conserved cold shock domain and nucleic acid binding motifs. A tertiary model of Dm-Csp1 revealed an anticipated Csp structure containing five anti-parallel beta-strands, and ligand prediction experiments identified N-terminally located residues capable of binding single-stranded nucleic acids. Putative Csps were identified from 100% of (27 of 27) Deinococci species for which genome information is available; and the Deinococci-encoded Csps identified contain a C-terminally located region that appears to be limited to members of the class Deinococci.

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 Assessing nucleic acid binding activity of four dinoflagellate cold shock domain proteins from Symbiodinium kawagutii and Lingulodinium polyedra

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Bahareh Zaheri ◽  
David Morse
Keyword(s):  
Transcription Factors ◽  
Nucleic Acid ◽  
Transcriptional Control ◽  
Cold Shock ◽  
Binding Activity ◽  
Dependent Manner ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Double Stranded Dna ◽  
Cold Shock Domain

Abstract Background Dinoflagellates have a generally large number of genes but only a small percentage of these are annotated as transcription factors. Cold shock domain (CSD) containing proteins (CSPs) account for roughly 60% of these. CSDs are not prevalent in other eukaryotic lineages, perhaps suggesting a lineage-specific expansion of this type of transcription factors in dinoflagellates, but there is little experimental data to support a role for dinoflagellate CSPs as transcription factors. Here we evaluate the hypothesis that dinoflagellate CSPs can act as transcription factors by binding double-stranded DNA in a sequence dependent manner. Results We find that both electrophoretic mobility shift assay (EMSA) competition experiments and selection and amplification binding (SAAB) assays indicate binding is not sequence specific for four different CSPs from two dinoflagellate species. Competition experiments indicate all four CSPs bind to RNA better than double-stranded DNA. Conclusion Dinoflagellate CSPs do not share the nucleic acid binding properties expected for them to function as bone fide transcription factors. We conclude the transcription factor complement of dinoflagellates is even smaller than previously thought suggesting that dinoflagellates have a reduced dependance on transcriptional control compared to other eukaryotes.

scholarly journals Cold Shock Proteins and Low-Temperature Response ofStreptococcus thermophilus CNRZ302

1999 ◽  
Vol 65 (10) ◽  
pp. 4436-4442 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Frank M. Rombouts ◽  
Willem M. de Vos ◽  
Oscar P. Kuipers ◽  
Tjakko Abee
Keyword(s):  
Low Temperature ◽  
Cold Shock ◽  
Thermophilic Bacterium ◽  
Temperature Adaptation ◽  
Transcriptional Level ◽  
Minimal Growth ◽  
Two Dimensional Gel Electrophoresis ◽  
Cold Shock Proteins ◽  
Shock Proteins ◽  
Induced Proteins

ABSTRACT Low-temperature adaptation and cryoprotection were studied in the thermophilic lactic acid bacterium Streptococcus thermophilus CNRZ302. S. thermophilus actively adapts to freezing during a pretreatment at 20°C, resulting in an approximately 1,000-fold increased survival after four freeze-thaw cycles compared to mid-exponential-phase cells grown at an optimal temperature of 42°C. No adaptation is observed when cells are exposed to a temperature (10°C) below the minimal growth temperature of the strain (just below 15°C). By two-dimensional gel electrophoresis several 7-kDa cold-induced proteins were identified, which are the major induced proteins after a shift to 20°C. These cold shock proteins were maximally expressed at 20°C, while the induction level was low after cold shock to 10°C. To confirm the presence ofcsp genes in S. thermophilus, a PCR strategy was used which yielded products of different sizes. Sequence analysis revealed csp-like sequences that were up to 95% identical to those of csp genes of S. thermophilus ST1-1,Streptococcus dysgalactiae, Streptococcus pyogenes, and Lactococcus lactis. Northern blot analysis revealed a seven- to ninefold induction of cspmRNA after a temperature shift to 20°C, showing that this thermophilic bacterium indeed contains at least one cold-induciblecsp gene and that its regulation takes place at the transcriptional level.

scholarly journals Structure and Function of Cold Shock Proteins in Archaea

2007 ◽  
Vol 189 (15) ◽  
pp. 5738-5748 ◽  
Author(s):  
Laura Giaquinto ◽  
Paul M. G. Curmi ◽  
Khawar S. Siddiqui ◽  
Anne Poljak ◽  
Ed DeLong ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Cold Adaptation ◽  
Biochemical Analysis ◽  
Cold Shock ◽  
Growth Defect ◽  
Nucleic Acid Binding ◽  
Cold Shock Proteins ◽  
E Coli ◽  
Structural And Functional Properties ◽  
Shock Proteins

ABSTRACT Archaea are abundant and drive critical microbial processes in the Earth's cold biosphere. Despite this, not enough is known about the molecular mechanisms of cold adaptation and no biochemical studies have been performed on stenopsychrophilic archaea (e.g., Methanogenium frigidum). This study examined the structural and functional properties of cold shock proteins (Csps) from archaea, including biochemical analysis of the Csp from M. frigidum. csp genes are present in most bacteria and some eucarya but absent from most archaeal genome sequences, most notably, those of all archaeal thermophiles and hyperthermophiles. In bacteria, Csps are small, nucleic acid binding proteins involved in a variety of cellular processes, such as transcription. In this study, archaeal Csp function was assessed by examining the ability of csp genes from psychrophilic and mesophilic Euryarchaeota and Crenarchaeota to complement a cold-sensitive growth defect in Escherichia coli. In addition, an archaeal gene with a cold shock domain (CSD) fold but little sequence identity to Csps was also examined. Genes encoding Csps or a CSD structural analog from three psychrophilic archaea rescued the E. coli growth defect. The three proteins were predicted to have a higher content of solvent-exposed basic residues than the noncomplementing proteins, and the basic residues were located on the nucleic acid binding surface, similar to their arrangement in E. coli CspA. The M. frigidum Csp was purified and found to be a single-domain protein that folds by a reversible two-state mechanism and to exhibit a low conformational stability typical of cold-adapted proteins. Moreover, M. frigidum Csp was characterized as binding E. coli single-stranded RNA, consistent with its ability to complement function in E. coli. The studies show that some Csp and CSD fold proteins have retained sufficient similarity throughout evolution in the Archaea to be able to function effectively in the Bacteria and that the function of the archaeal proteins relates to cold adaptation. The initial biochemical analysis of M. frigidum Csp has developed a platform for further characterization and demonstrates the potential for expanding molecular studies of proteins from this important archaeal stenopsychrophile.

scholarly journals Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

2021 ◽  
Vol 9 (5) ◽  
pp. 1061
Author(s):  
Francis Muchaamba ◽  
Roger Stephan ◽  
Taurai Tasara
Keyword(s):  
Listeria Monocytogenes ◽  
Stress Tolerance ◽  
Cold Shock ◽  
Current Data ◽  
Health Concern ◽  
Stress Exposure ◽  
Cold Shock Proteins ◽  
Cell Functions ◽  
Small Proteins ◽  
Shock Proteins

Listeria monocytogenes has evolved an extensive array of mechanisms for coping with stress and adapting to changing environmental conditions, ensuring its virulence phenotype expression. For this reason, L. monocytogenes has been identified as a significant food safety and public health concern. Among these adaptation systems are cold shock proteins (Csps), which facilitate rapid response to stress exposure. L. monocytogenes has three highly conserved csp genes, namely, cspA, cspB, and cspD. Using a series of csp deletion mutants, it has been shown that L. monocytogenes Csps are important for biofilm formation, motility, cold, osmotic, desiccation, and oxidative stress tolerance. Moreover, they are involved in overall virulence by impacting the expression of virulence-associated phenotypes, such as hemolysis and cell invasion. It is postulated that during stress exposure, Csps function to counteract harmful effects of stress, thereby preserving cell functions, such as DNA replication, transcription and translation, ensuring survival and growth of the cell. Interestingly, it seems that Csps might suppress tolerance to some stresses as their removal resulted in increased tolerance to stresses, such as desiccation for some strains. Differences in csp roles among strains from different genetic backgrounds are apparent for desiccation tolerance and biofilm production. Additionally, hierarchical trends for the different Csps and functional redundancies were observed on their influences on stress tolerance and virulence. Overall current data suggest that Csps have a wider role in bacteria physiology than previously assumed.

scholarly journals RNA target profiles direct the discovery of virulence functions for the cold-shock proteins CspC and CspE

2017 ◽  
pp. 201620772 ◽  
Author(s):  
Charlotte Michaux ◽  
Erik Holmqvist ◽  
Erin Vasicek ◽  
Malvika Sharan ◽  
Lars Barquist ◽  
...  
Keyword(s):  
Cold Shock ◽  
Cold Shock Proteins ◽  
Shock Proteins
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