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 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

scholarly journals Role of the Cys 2-Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1

1994 ◽  
Vol 3 (2) ◽  
pp. 227-239 ◽  
Author(s):  
Lorenz M. Mayr ◽  
Dieter Willbold ◽  
Olfert Landt ◽  
Franz X. Schmidm
Keyword(s):  
Disulfide Bond ◽  
Structure Stability ◽  
Folding Kinetics ◽  
Ribonuclease T1 ◽  
Kinetics Of

scholarly journals Role of folding kinetics of secondary structures in telomeric G-overhangs in the regulation of telomere maintenance in Saccharomyces cerevisiae

2020 ◽  
Vol 295 (27) ◽  
pp. 8958-8971 ◽  
Author(s):  
Katarina Jurikova ◽  
Martin Gajarsky ◽  
Mona Hajikazemi ◽  
Jozef Nosek ◽  
Katarina Prochazkova ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secondary Structures ◽  
Telomere Maintenance ◽  
Folding Kinetics ◽  
Mobility Shift ◽  
Dna Structures ◽  
Electrophoretic Mobility Shift Assays ◽  
Kinetics Of

The ends of eukaryotic chromosomes typically contain a 3′ ssDNA G-rich protrusion (G-overhang). This overhang must be protected against detrimental activities of nucleases and of the DNA damage response machinery and participates in the regulation of telomerase, a ribonucleoprotein complex that maintains telomere integrity. These functions are mediated by DNA-binding proteins, such as Cdc13 in Saccharomyces cerevisiae, and the propensity of G-rich sequences to form various non-B DNA structures. Using CD and NMR spectroscopies, we show here that G-overhangs of S. cerevisiae form distinct Hoogsteen pairing–based secondary structures, depending on their length. Whereas short telomeric oligonucleotides form a G-hairpin, their longer counterparts form parallel and/or antiparallel G-quadruplexes (G4s). Regardless of their topologies, non-B DNA structures exhibited impaired binding to Cdc13 in vitro as demonstrated by electrophoretic mobility shift assays. Importantly, whereas G4 structures formed relatively quickly, G-hairpins folded extremely slowly, indicating that short G-overhangs, which are typical for most of the cell cycle, are present predominantly as single-stranded oligonucleotides and are suitable substrates for Cdc13. Using ChIP, we show that the occurrence of G4 structures peaks at the late S phase, thus correlating with the accumulation of long G-overhangs. We present a model of how time- and length-dependent formation of non-B DNA structures at chromosomal termini participates in telomere maintenance.

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 The Role of Electrostatic Relaxation on the Folding Kinetics of a Bacterial Ribozyme

2011 ◽  
Vol 100 (3) ◽  
pp. 236a
Author(s):  
Joon Ho Roh ◽  
Robert M. Briber ◽  
Duncan Kilburn ◽  
Reza Behrouzi ◽  
Liang Guo ◽  
...  
Keyword(s):  
Folding Kinetics ◽  
Kinetics Of

scholarly journals A cold shock protein from a thermophile bacterium promotes the high-temperature growth of bacteria and fungi through binding to diverse RNA species

2019 ◽  
Author(s):  
Zikang Zhou ◽  
Hongzhi Tang ◽  
Weiwei Wang ◽  
Lige Zhang ◽  
Fei Su ◽  
...  
Keyword(s):  
High Temperature ◽  
High Temperatures ◽  
Cold Shock ◽  
Nucleotide Binding ◽  
Cold Shock Protein ◽  
Ecological Niches ◽  
Variant Form ◽  
Thermophilic Microorganisms ◽  
Temperature Growth ◽  
Biomass Increase

AbstractHigh temperatures deleteriously affect cells by damaging cellular structures and changing the behavior of diverse biomolecules, and extensive research about thermophilic microorganisms has elucidated some of the mechanisms that can overcome these effects and allow thriving in high-temperature ecological niches. We here used functional genomics methods to screen out a cold-shock protein (CspL) from a high-productivity lactate producing thermophile strain (Bacillus coagulans strain 2-6) grown at 37°C and 60°C. We subsequently made the highly striking finding that transgenic expression of CspL conferred massive increases in high temperature growth of other organisms including E. coli (2.4-fold biomass increase at 45°C) and the eukaryote S. cerevisiae (a 2.7-fold biomass increase at 34°C). Pursuing these findings, we used bio-layer interferometry assays to characterize the nucleotide-binding function of CspL in vitro, and used proteomics and RNA-Seq to characterize the global effects of CspL on mRNA transcript accumulation and used RIP-Seq to identify in vivo RNA targets of this nucleotide-binding protein (e.g. rpoE, and rmf, etc.). Finally, we confirmed that a nucleotide-binding-dead variant form of CspL does not have increased growth rates or biomass accumulation effects at high temperatures. Our study thus establishes that CspL can function as a global RNA chaperone.

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.

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