Role of the Chain Termini for the Folding Transition State of the Cold Shock Protein†

Biochemistry ◽  
2001 ◽  
Vol 40 (51) ◽  
pp. 15501-15511 ◽  
Author(s):  
Dieter Perl ◽  
Georg Holtermann ◽  
Franz X. Schmid
Keyword(s):  
Transition State ◽  
Cold Shock ◽  
Cold Shock Protein

The Folding Transition State of the Cold Shock Protein is Strongly Polarized

2004 ◽  
Vol 339 (3) ◽  
pp. 555-569 ◽  
Author(s):  
Maria M Garcia-Mira ◽  
Daniel Boehringer ◽  
Franz X Schmid
Keyword(s):  
Transition State ◽  
Cold Shock ◽  
Cold Shock Protein

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.

Role of Entropy in Protein Thermostability:  Folding Kinetics of a Hyperthermophilic Cold Shock Protein at High Temperatures Using19F NMR†

Biochemistry ◽  
2002 ◽  
Vol 41 (39) ◽  
pp. 11670-11680 ◽  
Author(s):  
Benjamin Schuler ◽  
Werner Kremer ◽  
Hans Robert Kalbitzer ◽  
Rainer Jaenicke
Keyword(s):  
High Temperatures ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Folding Kinetics ◽  
Protein Thermostability ◽  
Kinetics Of

scholarly journals Assessing the role of cold-shock protein C: A novel regulator of Acinetobacter baumannii biofilm formation and virulence

2021 ◽  
Author(s):  
Brooke Tomlinson ◽  
Grant A Denham ◽  
Robert Brzozowski ◽  
Jessie L Allen ◽  
Prahathees J. Eswara ◽  
...  
Keyword(s):  
Acinetobacter Baumannii ◽  
Biofilm Formation ◽  
Protein C ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Resistant Isolate ◽  
Healthcare Personnel ◽  
Human Immune System ◽  
Altered Expression

Acinetobacter baumannii is a formidable opportunistic pathogen that is notoriously difficult to eradicate from hospital settings and can spread quickly via healthcare personnel despite preventive measures. This resilience is often attributed to a proclivity for biofilm formation, which grants A. baumannii a higher tolerance towards external stress, desiccation, and antimicrobials. Despite this, little is known regarding the mechanisms orchestrating A. baumannii biofilm formation. Herein, we performed RNA-seq on biofilm and planktonic populations for the multidrug resistant isolate, AB5075, and identified 438 genes with altered expression. To assess the potential role of genes upregulated within biofilms, we tested the biofilm forming capacity of their respective mutants from an A. baumannii transposon library. In so doing, we uncovered 24 genes whose disruption led to reduced biofilm formation. One such element, cold shock protein C (cspC), produced a mucoidal, non-mucoviscous colony phenotype. RNA-sequencing of this mutant revealed the down regulation of pili and fimbriae in the cspC mutant, which would explain the decreased biofilm observed. Using MIC assays, we note that the mutant displayed increased antibiotic tolerance that we hypothesize is mediated by overexpression of multi-drug efflux pumps and altered mRNA stability of their corresponding transcriptional repressor. Finally, we show that CspC is required for survival during oxidative stress and challenge by the human immune system, and plays a pivotal role during systemic infection. Collectively, our work identifies a cadre of new biofilm associated genes within A. baumannii and provides insight into the global regulatory network of this emerging human pathogen.

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
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