Cold denaturation of proteins under high pressure

Kunugi, Shigeru; Tanaka, Naoki

doi:10.1016/s0167-4838(01)00354-5

Cited by 140 publications

(101 citation statements)

References 65 publications

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“…In most cases the loss of activity is followed by dissociation into monomers, a process which can be reversed by rewarming; but in some cases it is followed by an aggregation step. 9,10,14 Reversible cold inactivation is believed to be of physiological significance. For example, tetramer-dimer equilibrium of phosphofructokinase was suggested as a factor responsible for a relative decrease in the contribution of glycolysis to overall energy production during hibernation in ground squirrels and European hamsters.…”

Section: Cold Inactivationmentioning

confidence: 99%

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

et al. 2007

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A wide variety of enzymes can undergo a reversible loss of activity at low temperature, a process that is termed cold inactivation. This phenomenon is found in oligomeric enzymes such as tryptophanase (Trpase) and other pyridoxal phosphate dependent enzymes. On the other hand, cold‐adapted, or psychrophilic enzymes, isolated from organisms able to thrive in permanently cold environments, have optimal activity at low temperature, which is associated with low thermal stability. Since cold inactivation may be considered “contradictory” to cold adaptation, we have looked into the amino acid sequences and the crystal structures of two families of enzymes, subtilisin and tryptophanase. Two cold adapted subtilisins, S41 and subtilisin‐like protease from Vibrio, were compared to a mesophilic and a thermophilic subtilisins, as well as to four PLP‐dependent enzymes in order to understand the specific surface residues, specific interactions, or any other molecular features that may be responsible for the differences in their tolerance to cold temperatures. The comparison between the psychrophilic and the mesophilic subtilisins revealed that the cold adapted subtilisins have a high content of acidic residues mainly found on their surface, making it charged. The analysis of the Trpases showed that they have a high content of hydrophobic residues on their surface. Thus, we suggest that the negatively charged residues on the surface of the subtilisins may be responsible for their cold adaptation, whereas the hydrophobic residues on the surface of monomeric Trpase molecules are responsible for the tetrameric assembly, and may account for their cold inactivation and dissociation. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 354–359, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Section: Cold Inactivationmentioning

confidence: 99%

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

et al. 2007

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“…The latter phenomenon, where the protein unfolds thereby increasing its entropy, is called cold denaturation and is accompanied by a decrease in the entropy of the entire system. This counterintuitive behavior has been experimentally verified [3,5] but has remained a subject of controversy [2,4], since a satisfactory microscopic explanation for this phenomenon has not yet emerged. Resolving cold denaturation microscopically would facilitate understanding the forces responsible for the structure of proteins and, in particular, the role of the complex hydrophobic effect.…”

mentioning

confidence: 93%

“…Hence, increasing pressure and decreasing temperature destabilize hydrophobic contacts in favor of similar solvent-separated configurations. We expect that this aggravated destabilization of hydrophobic contacts at high pressure explains why the transition temperature for cold denaturation increases with increasing pressure [2]. Here, we study cold denaturation at the equivalent of ambient pressure.…”

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confidence: 97%

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Microscopic Mechanism for Cold Denaturation

et al. 2008

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We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.

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“…Our previous work has shown that exposure of Envs to 0°C, which is thought to destabilize protein structure by promoting hydration of hydrophobic residues (26,27), can inactivate the infectivity of some HIV-1 isolates (23,28). Strains that are cold sensitive are often also globally sensitive to antibody neutralization (23).…”

mentioning

confidence: 99%

Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States

Johnson

Zhai

Salehiniya

et al. 2017

J Virol

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The envelope glycoproteins (Envs) on the surfaces of HIV-1 particles are targeted by host antibodies. Primary HIV-1 isolates demonstrate different global sensitivities to antibody neutralization; tier-1 isolates are sensitive, whereas tier-2 isolates are more resistant. Single-site mutations in Env can convert tier-2 into tier-1-like viruses. We hypothesized that such global change in neutralization sensitivity results from weakening of intramolecular interactions that maintain Env integrity. Three strategies commonly applied to perturb protein structure were tested for their effects on global neutralization sensitivity: exposure to low temperature, Envactivating ligands, and a chaotropic agent. A large panel of diverse tier-2 isolates from clades B and C was analyzed. Incubation at 0°C, which globally weakens hydrophobic interactions, causes gradual and reversible exposure of the coreceptorbinding site. In the cold-induced state, Envs progress at isolate-specific rates to unstable forms that are sensitive to antibody neutralization and then gradually lose function. Agents that mimic the effects of CD4 (CD4Ms) also induce reversible structural changes to states that exhibit isolate-specific stabilities. The chaotropic agent urea (at low concentrations) does not affect the structure or function of native Env. However, urea efficiently perturbs metastable states induced by cold and CD4Ms and increases their sensitivity to antibody neutralization and their inactivation rates Therefore, chemical and physical agents can guide Env from the stable native state to perturbation-sensitive forms and modulate their stability to bestow tier-1-like properties on primary tier-2 strains. These concepts can be applied to enhance the potency of vaccine-elicited antibodies and microbicides at mucosal sites of HIV-1 transmission.IMPORTANCE An effective vaccine to prevent transmission of HIV-1 is a primary goal of the scientific and health care communities. Vaccine-elicited antibodies target the viral envelope glycoproteins (Envs) and can potentially inhibit infection. However, the potency of such antibodies is generally low. Single-site mutations in Env can enhance the global sensitivity of HIV-1 to neutralization by antibodies. We found that such a hypersensitivity phenotype can also be induced by agents that destabilize protein structure. Exposure to 0°C or low concentrations of Env-activating ligands gradually guides Env to metastable forms that expose cryptic epitopes and that are highly sensitive to neutralization. Low concentrations of the chaotropic agent urea do not affect native Env but destabilize perturbed states induced by cold or CD4Ms and increase their neutralization. The concept of enhancing antibody sen-

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Cold denaturation of proteins under high pressure

Cited by 140 publications

References 65 publications

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

Microscopic Mechanism for Cold Denaturation

Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States

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