Role of electrostatic interactions for the stability and folding behavior of cold shock protein

2010 ◽  
pp. NA-NA ◽  
Author(s):  
Ji Guo Su ◽  
Wei Zu Chen ◽  
Cun Xin Wang
Keyword(s):  
Electrostatic Interactions ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
The Stability

scholarly journals Human DNA Telomeres in Presence of Oxidative Lesions: The Crucial Role of Electrostatic Interactions on the Stability of Guanine Quadruplexes

Antioxidants ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 337 ◽  
Author(s):  
Hognon ◽  
Gebus ◽  
Barone ◽  
Monari
Keyword(s):  
Electrostatic Interactions ◽  
Empty Site ◽  
Quadruplex Structure ◽  
Abasic Sites ◽  
Human Dna ◽  
Guanine Quadruplex ◽  
Guanine Base ◽  
The Stability ◽  
Dynamics Simulations

By using all atom molecular dynamics simulations, we studied the behavior of human DNA telomere sequences in guanine quadruplex (G4) conformation and in the presence of oxidative lesions, namely abasic sites. In particular, we evidenced that while removing one guanine base induces a significant alteration and destabilization of the involved leaflet, human telomere oligomers tend, in most cases, to maintain at least a partial quadruplex structure, eventually by replacing the empty site with undamaged guanines of different leaflets. This study shows that (i) the disruption of the quadruplex leaflets induces the release of at least one of the potassium cations embedded in the quadruplex channel and that (ii) the electrostatic interactions of the DNA sequence with the aforementioned cations are fundamental to the maintenance of the global quadruplex structure.

scholarly journals Mutation Analysis of the 5′ Untranslated Region of the Cold Shock cspA mRNA of Escherichia coli

1999 ◽  
Vol 181 (20) ◽  
pp. 6284-6291 ◽  
Author(s):  
Kunitoshi Yamanaka ◽  
Masanori Mitta ◽  
Masayori Inouye
Keyword(s):  
Escherichia Coli ◽  
Untranslated Region ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Translation Efficiency ◽  
Negative Effect ◽  
Downstream Box ◽  
The Stability ◽  
The Relationship ◽  
Positive Effect

ABSTRACT The mRNA for CspA, a major cold shock protein in Escherichia coli, contains an unusually long (159 bases) 5′ untranslated region (5′-UTR), and its stability has been shown to play a major role in cold shock induction of CspA. The 5′-UTR of the cspAmRNA has a negative effect on its expression at 37°C but has a positive effect upon cold shock. In this report, a series ofcspA-lacZ fusions having a 26- to 32-base deletion in the 5′-UTR were constructed to examine the roles of specific regions within the 5′-UTR in cspA expression. It was found that none of the deletion mutations had significant effects on the stability of mRNA at both 37 and 15°C. However, two mutations (Δ56-86 and Δ86-117) caused a substantial increase of β-galactosidase activity at 37°C, indicating that the deleted regions contain a negativecis element(s) for translation. A mutation (Δ2-27) deleting the highly conserved cold box sequence had little effect on cold shock induction of β-galactosidase. Interestingly, three mutations (Δ28-55, Δ86-117, and Δ118-143) caused poor cold shock induction of β-galactosidase. In particular, the Δ118-143 mutation reduced the translation efficiency of the cspA mRNA to less than 10% of that of the wild-type construct. The deleted region contains a 13-base sequence named upstream box (bases 123 to 135), which is highly conserved in cspA, cspB,cspG, and cspI, and is located 11 bases upstream of the Shine-Dalgarno (SD) sequence. The upstream box might be another cis element involved in translation efficiency of the cspA mRNA in addition to the SD sequence and the downstream box sequence. The relationship between the mRNA secondary structure and translation efficiency is discussed.

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

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 Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: the Role of pH

Molecules ◽  
2020 ◽  
Vol 25 (17) ◽  
pp. 3871
Author(s):  
Ziyuan Wang ◽  
Jie Liu ◽  
Jian Gao ◽  
Mengna Cao ◽  
Gerui Ren ◽  
...  
Keyword(s):  
Targeted Delivery ◽  
Electrostatic Interactions ◽  
Driving Forces ◽  
Gum Arabic ◽  
Soluble Polymers ◽  
Food Research ◽  
The Stability ◽  
Β Lactoglobulin

Protein–polysaccharide complexes have received increasing attention as delivery systems to improve the stability and bioavailability of multiple bioactive compounds. However, deep and comprehensive understanding of the interactions between proteins and polysaccharides is still required for enhancing their loading efficiency and facilitating targeted delivery. In this study, we fabricated a type of protein–polysaccharide complexes using food-grade materials of β-lactoglobulin (β-Lg) and gum arabic (GA). The formation and characteristics of β-Lg–GA complexes were investigated by determining the influence of pH and other factors on their turbidity, zeta-potential, particle size and rheology. Results demonstrated that the β-Lg and GA suspension experienced four regimes including co-soluble polymers, soluble complexes, insoluble complexes and co-soluble polymers when the pH ranged from 1.2 to 7 and that β-Lg–GA complexes formed in large quantities at pH 4.2. An increased ratio of β-Lg in the mixtures was found to promote the formation of β-Lg and GA complexes, and the optimal β-Lg/GA ratio was found to be 2:1. The electrostatic interactions between the NH3+ group in β-Lg and the COO− group in GA were confirmed to be the main driving forces for the formation of β-Lg/GA complexes. The formed structure also resulted in enhanced thermal stability and viscosity. These findings provide critical implications for the application of β-lactoglobulin and gum arabic complexes in food research and industry.

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