The thermal stability of turnip yellow mosaic virus under hydrostatic pressure

Goldbeck, A.; Lechner, M. D.; Witz, Jean‐François; Nordmeier, E. H.; Ibel, K.

doi:10.1007/bf01561137

Cited by 10 publications

(2 citation statements)

References 26 publications

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“…Turnip yellow mosaic virus, for example, is stabilized by hydrostatic pressure against the thermally induced uncoating of its RNA. (Goldbeck et al, 1991). Considering the endothermic association of TMV protein (Jaenicke and Lauffer, 1969;Sturtevant et al, 1981;Jaenicke, 1991a), it seems as if different kinds of interactions dominated in both cases.…”

Section: Nucleoproteins and Assembly Systenzsmentioning

confidence: 99%

Proteins under pressure

Groß

Jaenicke

1994

European Journal of Biochemistry

661

393

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Oceans not only cover the major part of the earth's surface but also reach into depths exceeding the height of the Mt Everest. They are populated down to the deepest levels (=11800 m), which means that a significant proportion of the global biosphere is exposed to pressures of up to 120 MPa. Although this fact has been known for more than a century, the ecology of the 'abyss' is still in its infancy. Only recently, barophilic adaptation, i.e. the requirement of elevated pressure for viability, has been firmly established. In non-adapted organisms, increased pressure leads to morphological anomalies or growth inhibition, and ultimately to cell death. The detailed molecular mechanism of the underlying 'metabolic dislocation' is unresolved.Effects of pressure as a variable in microbiology, biochemistry and biotechnology allow the structure/function relationship of proteins and protein conjugates to be analyzed. In this context, stabilization by cofactors or accessory proteins has been observed. High-pressure equipment available today allows the comprehensive characterization of the behaviour of proteins under pressure. Single-chain proteins undergo pressure-induced denaturation in the 100-MPa range, which, in the case of oligomeric proteins or protein assemblies, is preceded by dissociation at lower pressure. The effects may be ascribed to the positive reaction volumes connected with the formation of hydrophobic and ionic interactions. In addition, the possibility of conformational effects exerted by moderate, non-denaturing pressures, and related to the intrinsic compressibility of proteins, is discussed. Crystallization may serve as a model reaction of protein self-organization. Kinetic aspects of its pressureinduced inhibition can be described by a model based on the Oosawa theory of molecular association. Barosensitivity is known to be correlated with the pressure-induced inhibition of protein biosynthesis. Attempts to track down the ultimate cause in the dissociation of ribosomes have revealed remarkable stabilization of functional complexes under pseudo-physiological conditions, with the post-translational complex as the most pressure-sensitive species. Apart from the key issue of barosensitivity and barophilic adaptation, high-pressure biochemistry may provide means to develop new approaches to nonthermic industrial processes, especially in the field of food technology.Life in the deep sea faces a whole set of unfavourable conditions, including pressures up to 120 MPa (1200 bar), temperatures around 2°C or, in volcanic regions, above 1OO"C, absence of sunlight, and scarce supply of organic nutrients. When 'deep' means deeper than 1000 m, these biotopes include more than half (~6 2 % ) of the volume of the global biosphere (Jannasch and Taylor, 1984). The average pressure on the ocean floor is of the order of 38 MPa, indicatCorrespondence to R. Jaenicke,

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Section: Nucleoproteins and Assembly Systenzsmentioning

confidence: 99%

Proteins under pressure

Groß

Jaenicke

1994

European Journal of Biochemistry

661

393

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“…Prior to P\T treatments, the enzyme preparation was 3-fold diluted in 20 mM Bis-Tris buffer, pH 7.0. Bis-Tris buffer was chosen because its protonic activity is almost invariant with both the temperature : dpK a(Bis-Tris) \dT l k0.017 K −" and the pressure dpH\dP l k0.055 kbar −" [32,33].…”

Section: P/t Treatment Of the Enzymementioning

confidence: 99%

Pressure- and heat-induced inactivation of butyrylcholinesterase: evidence for multiple intermediates and the remnant inactivation process

Weingand-Ziadé¹,

Ribes²,

Renault³

et al. 2001

Biochem. J.

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The inactivation process of native (N) human butyrylcholinesterase (BuChE) by pressure and/or heat was found to be multi-step. It led to irreversible formation of an active intermediate (I) state and a denatured state. This series-inactivation process was described by expanding the Lumry-Eyring [Lumry, R. and Eyring, H. (1954) J. Phys. Chem. 58, 110-120] model. The intermediate state (I) was found to have a K(m) identical with that of the native state and a turnover rate (k(cat)) twofold higher than that of the native state with butyrylthiocholine as the substrate. The increased catalytic efficiency (k(cat)/K(m)) of I can be explained by a conformational change in the active-site gorge and/or restructuring of the water-molecule network in the active-site pocket, making the catalytic steps faster. However, a pressure/heat-induced covalent modification of native BuChE, affecting the catalytic machinery, cannot be ruled out. The inactivation process of BuChE induced by the combined action of pressure and heat was found to continue after interruption of pressure/temperature treatment. This secondary inactivation process was termed 'remnant inactivation'. We hypothesized that N and I were in equilibrium with populated metastable N' and I' states. The N' and I' states can either return to the active forms, N and I, or develop into inactive forms, N(')(in) and I(')(in). Both active N' and I' intermediate states displayed different rates of remnant inactivation depending on the pressure and temperature pretreatments and on the storage temperature. A first-order deactivation model describing the kinetics of the remnant inactivation of BuChE is proposed.

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