Dissociative mechanism of F-actin thermal denaturation

Mikhailova, V. V.; Bi, Kurganov; Pivovarova, Anastasia V.; Levitsky, Dmitrii I.

doi:10.1134/s0006297906110125

Cited by 12 publications

(28 citation statements)

References 41 publications

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“…Surprisingly, our DSC experiments have shown that the thermal stability of F‐actin depends strongly on the concentration of ADP added. The transition temperature ( T m ) of F‐actin increased by 5–6 °C with increasing ADP concentrations up to 1 m m , and reached a plateau at higher ADP concentrations, a half‐maximum increase in T m being observed in the presence of 0.1 m m ADP [46]. The stabilizing effect of ADP was highly specific, being observed only with ADP, and not with other nucleoside diphosphates (IDP, UDP, GDP, CDP).…”

Section: Thermal Unfolding Of F‐actin Filamentsmentioning

confidence: 99%

“…A similar effect of the F‐actin thermal stabilization was also seen in the presence of ATP; however, this effect was much less specific, and was observed, although to a lesser extent, for other nucleoside triphosphates (ITP, UTP and GTP). Another difference between the effects of ATP and ADP was that an increase in ATP concentration from 1 to 5 m m led to further significant increase in the thermal stability of F‐actin ( T m increased by > 3 °C), whereas a similar increase in ADP concentration had no influence on the thermal unfolding of F‐actin [46]. These findings suggest that the stabilizing effect of ATP [46,47] differs significantly in its mechanism from the effect caused by ADP [46].…”

Section: Thermal Unfolding Of F‐actin Filamentsmentioning

confidence: 99%

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Thermal unfolding and aggregation of actin

et al. 2008

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Actin is one of the most abundant proteins in nature. It is found in all eukaryotes and plays a fundamental role in many diverse and dynamic cellular processes. Also, actin is one of the most ubiquitous proteins because actin‐like proteins have recently been identified in bacteria. Actin filament (F‐actin) is a highly dynamic structure that can exist in different conformational states, and transitions between these states may be important in cytoskeletal dynamics and cell motility. These transitions can be modulated by various factors causing the stabilization or destabilization of actin filaments. In this review, we look at actin stabilization and destabilization as expressed by changes in the thermal stability of actin; specifically, we summarize and analyze the existing data on the thermal unfolding of actin as measured by differential scanning calorimetry. We also analyze in vitro data on the heat‐induced aggregation of actin, the process that normally accompanies actin thermal denaturation. In this respect, we focus on the effects of small heat shock proteins, which can prevent the aggregation of thermally denatured actin with no effect on actin thermal unfolding. As a result, we have proposed a mechanism describing the thermal denaturation and aggregation of F‐actin. This mechanism explains some of the special features of the thermal unfolding of actin filaments, including the effects of their stabilization and destabilization; it can also explain how small heat shock proteins protect the actin cytoskeleton from damage caused by the accumulation of large insoluble aggregates under heat shock conditions.

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Section: Thermal Unfolding Of F‐actin Filamentsmentioning

confidence: 99%

Section: Thermal Unfolding Of F‐actin Filamentsmentioning

confidence: 99%

Thermal unfolding and aggregation of actin

et al. 2008

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“…Mikhailova et al [13] demonstrated that the transition temperature of F-actin was strongly dependent on the concentration of both ADP and actin. Based on their observations, the authors proposed a ''dissociative'' mechanism for thermal denaturation of F-actin.…”

Section: Discussionmentioning

confidence: 98%

“…The similarity in activation energy between the two actins suggests that the rapid thermal denaturation of carp F-actin was caused by a large ''frequency factor.'' Mikhailova et al [13] have proposed that two molecular processes precede irreversible thermal denaturation of F-actin. One is fragmentation of F-actin and the other is dissociation of bound nucleotides from the fragments (see ''Discussion'' section).…”

Section: Comparison Of Thermal Denaturation Rate Between Carp and Chimentioning

confidence: 99%

Thermal stability of carp actin in its polymerized form

Ooi

Okagaki

2011

Fish Sci

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We investigated the thermal denaturation of carp F-actin by measuring the loss of polymerization ability. The thermal denaturation rates of carp F-actin were at least 10-fold higher than those of chicken F-actin. Binding of tropomyosin thermally stabilized carp F-actin with no appreciable change in activation energy, suggesting the instability was caused by a high frequency of fragmentation of the actin filaments. A comparison of the critical concentration for polymerization suggested that the subunit-subunit interactions of carp F-actin were indeed weaker than those of chicken F-actin. Furthermore, using fluorescence quenching we showed that the nucleotide binding region of carp F-actin was in a more open conformation. Together, our results suggest that the instability of carp F-actin is a function of both the rate of fragmentation and the dissociation of bound nucleotides.

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“…The analogous change in DSC profiles with varying protein concentrations were obtained for other dissociating protein Residues and structural elements of the subunit A′ are designated by primes. The figure is generated by using the MolBrowser 3.8-4a software (MolSoft) (Surolia et al 1996), winged bean acidic lectin (Srinivas et al 1998), Phb from rabbit skeletal muscles , filamentous actin (Mikhailova et al 2006), Entamoeba histolytica triosephosphate isomerase (Tellez et al 2008) and extracellular hemoglobin of Glossoscolex paulistus (Santiago et al 2010). …”

Section: Dissociative Mechanism For Irreversible Thermal Denaturationmentioning

confidence: 99%

Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

2016

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Protein stability is a fundamental characteristic essential for understanding conformational transformations of the proteins in the cell. When using protein preparations in biotechnology and biomedicine, the problem of protein stability is of great importance. The kinetics of denaturation of oligomeric proteins may have characteristic properties determined by the quaternary structure. The kinetic schemes of denaturation can include the multiple stages of conformational transitions in the protein oligomer and stages of reversible dissociation of the oligomer. In this case, the shape of the kinetic curve of denaturation or the shape of the melting curve registered by differential scanning calorimetry can vary with varying the protein concentration. The experimental data illustrating dissociative mechanism for irreversible thermal denaturation of oligomeric proteins have been summarized in the present review. The use of test systems based on thermal aggregation of oligomeric proteins for screening of agents possessing anti-aggregation activity is discussed.

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Dissociative mechanism of F-actin thermal denaturation

Cited by 12 publications

References 41 publications

Thermal unfolding and aggregation of actin

Thermal unfolding and aggregation of actin

Thermal stability of carp actin in its polymerized form

Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

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