Cold shock proteins improve E. coli cell‐free synthesis in terms of soluble yields of aggregation‐prone proteins

2020 ◽  
Vol 117 (6) ◽  
pp. 1628-1639 ◽  
Author(s):  
Kae Higuchi ◽  
Takashi Yabuki ◽  
Masahiro Ito ◽  
Takanori Kigawa
Keyword(s):  
Cold Shock ◽  
Coli Cell ◽  
Cold Shock Proteins ◽  
E Coli ◽  
Shock Proteins

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 Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli

2017 ◽  
Vol 16 (10) ◽  
pp. 3722-3731 ◽  
Author(s):  
Nadia G. D’Lima ◽  
Alexandra Khitun ◽  
Aaron D. Rosenbloom ◽  
Peijia Yuan ◽  
Brandon M. Gassaway ◽  
...  
Keyword(s):  
Cold Shock ◽  
Comparative Proteomics ◽  
Cold Shock Proteins ◽  
E Coli ◽  
Shock Proteins

scholarly journals Insights into the Phylogeny and Evolution of Cold Shock Proteins: From Enteropathogenic Yersinia and Escherichia coli to Eubacteria

2019 ◽  
Vol 20 (16) ◽  
pp. 4059 ◽  
Author(s):  
Tao Yu ◽  
Riikka Keto-Timonen ◽  
Xiaojie Jiang ◽  
Jussa-Pekka Virtanen ◽  
Hannu Korkeala
Keyword(s):  
Escherichia Coli ◽  
Cold Shock ◽  
Phylogenetic Analyses ◽  
Recent Common Ancestor ◽  
Homologous Proteins ◽  
Cold Shock Proteins ◽  
E Coli ◽  
Most Recent Common Ancestor ◽  
Enteropathogenic Yersinia ◽  
Shock Proteins

Psychrotrophic foodborne pathogens, such as enteropathogenic Yersinia, which are able to survive and multiply at low temperatures, require cold shock proteins (Csps). The Csp superfamily consists of a diverse group of homologous proteins, which have been found throughout the eubacteria. They are related to cold shock tolerance and other cellular processes. Csps are mainly named following the convention of those in Escherichia coli. However, the nomenclature of certain Csps reflects neither their sequences nor functions, which can be confusing. Here, we performed phylogenetic analyses on Csp sequences in psychrotrophic enteropathogenic Yersinia and E. coli. We found that representative Csps in enteropathogenic Yersinia and E. coli can be clustered into six phylogenetic groups. When we extended the analysis to cover Enterobacteriales, the same major groups formed. Moreover, we investigated the evolutionary and structural relationships and the origin time of Csp superfamily members in eubacteria using nucleotide-level comparisons. Csps in eubacteria were classified into five clades and 12 subclades. The most recent common ancestor of Csp genes was estimated to have existed 3585 million years ago, indicating that Csps have been important since the beginning of evolution and have enabled bacterial growth in unfavorable conditions.

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 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 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

scholarly journals The Role of Electrostatics and Folding Kinetics on the Thermostability of Homologous Cold Shock Proteins

2020 ◽  
Vol 60 (2) ◽  
pp. 546-561 ◽  
Author(s):  
Paulo Henrique Borges Ferreira ◽  
Frederico Campos Freitas ◽  
Michelle E. McCully ◽  
Gabriel Gouvêa Slade ◽  
Ronaldo Junio de Oliveira
Keyword(s):  
Cold Shock ◽  
Folding Kinetics ◽  
Cold Shock Proteins ◽  
Shock Proteins

On Heat and Cells and Proteins

Physiology ◽  
2004 ◽  
Vol 19 (1) ◽  
pp. 11-15 ◽  
Author(s):  
Dörthe M. Katschinski
Keyword(s):  
Temperature Field ◽  
Heat Shock ◽  
Temperature Control ◽  
Cold Shock ◽  
Control Strategies ◽  
Cellular Function ◽  
The Body ◽  
Cold Shock Proteins ◽  
Shock Proteins

Two principal forms of temperature-control strategies have evolved, i.e., poikilothermic and homeothermic life. Even in homeothermic animals, the temperature field of the body is not homogenous. These observed temperature differences can affect cellular function directly or via the expression of heat shock or cold shock proteins.

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