Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase

Erijman, Leonardo; Lorimer, George H.; Weber, Gregorio

doi:10.1021/bi00070a030

Cited by 36 publications

(25 citation statements)

References 45 publications

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“…Oligomeric proteins can be dissociated by lower pressure than monomeric proteins; for example, in the GroEl chaperonin complex (14 subunits) from E. coli, dissociation occurred at 130 MPa (Gorovits et al 1995), while the RuBisCO from Rhodospirillum rubrum already started to dissociate at 40 MPa (Erijman et al 1993). Interestingly, these pressure values lie within the physiological range of many deep-sea organisms.…”

Section: Molecular Adaptation Of Deep-sea Enzymesmentioning

confidence: 93%

Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes

et al. 2015

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Prokaryotes inhabiting in the deep sea vent ecosystem will thus experience harsh conditions of temperature, pH, salinity or high hydrostatic pressure (HHP) stress. Among the fifty-two piezophilic and piezotolerant prokaryotes isolated so far from different deep-sea environments, only fifteen (four Bacteria and eleven Archaea) that are true hyper/thermophiles and piezophiles have been isolated from deep-sea hydrothermal vents; these belong mainly to the Thermococcales order. Different strategies are used by microorganisms to thrive in deep-sea hydrothermal vents in which "extreme" physico-chemical conditions prevail and where non-adapted organisms cannot live, or even survive. HHP is known to impact the structure of several cellular components and functions, such as membrane fluidity, protein activity and structure. Physically the impact of pressure resembles a lowering of temperature, since it reinforces the structure of certain molecules, such as membrane lipids, and an increase in temperature, since it will also destabilize other structures, such as proteins. However, universal molecular signatures of HHP adaptation are not yet known and are still to be deciphered.

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Section: Molecular Adaptation Of Deep-sea Enzymesmentioning

confidence: 93%

Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes

et al. 2015

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“…Fluorescence excitation and emission spectra of the protein-bis-ANS complex were collected at room temperature using a Shimadzu RF-5301PC spectrofluorometer as previously described [31,32]. Bis-ANS was excited with 360 nm light and the fluorescence emission collected from 370 nm to 600 nm.…”

Section: Fluorescence Measurementsmentioning

confidence: 99%

“…This fluorescent probe has been extensively used to study protein conformational states because it binds to solvent exposed hydrophobic pockets surrounded by positively charged residues [32,33]. Such binding dramatically increases the quantum yield, and shifts the max to shorter wavelengths.…”

Section: Fluorescence Spectroscopymentioning

confidence: 99%

Inhaled Anesthetic Modulation of Amyloid β 1-40 Assembly and Growth

Carnini¹,

Lear²,

Eckenhoff

2007

CAR

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Anesthesia and surgery have been reported to produce long-term cognitive problems, and to accelerate neurodegenerative disorders in the elderly. In previous work, we found that inhaled anesthetics enhance fibril formation and cytotoxicity of amyloid beta peptide. In this work we show that the inhaled anesthetics halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) and isoflurane (1-chloro-2,2,2-trifluoroethyl difluoromethyl ether) also favor intermediate oligomers of amyloid beta(1-40), and reduce solubility of amyloid beta(1-40) monomer. Size-exclusion chromatography, analytical ultracentrifugation and photo-induced cross-linking experiments indicate halothane enhancement of oligomeric species having molecular weight approximately 44-100 kDa. Bis-ANS fluorescence experiments revealed that halothane stabilizes a population of diffusible oligomers relative to the monomer or the mature fibril. These data show that inhaled anesthetics lower the amyloid beta(1-40) concentration necessary to initiate oligomer formation, probably by preferential binding to intermediate oligomers en route to fibril formation.

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“…For example, tetramers are proposed to exhibit an 'intermediate' behaviour between the classical 'stochastic' dissociation of dimers, and the 'deterministic' non-equilibrium dissociation found in large aggregates, e.g. in the extracellular hemoglobin of Glossoscolex paulistus (Silva et al, 1989;Erijman et al, 1993).…”

Section: Pressure-dependent Dissociation-associationmentioning

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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Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase

Cited by 36 publications

References 45 publications

Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes

Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes

Inhaled Anesthetic Modulation of Amyloid β 1-40 Assembly and Growth

Proteins under pressure

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