Role of water in some biological processes.

Wiggins, Philippa M.

doi:10.1128/mmbr.54.4.432-449.1990

Cited by 188 publications

(63 citation statements)

References 68 publications

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“…43 These denominations are much criticized nowadays, 44 as the differences found in the actual binding of these two water fractions are very small, if any at all. [45][46][47][48][49][50] For comparative purposes, Figure 5 shows typical calorimetric thermograms obtained during rewarming for the cryoprotective solutions used (at stages b-d), in the same conditions than those applied in the experiments of Figure 4.…”

Section: Measurement Of Ice Heat Of Fusion Using Dscmentioning

confidence: 99%

Glassy State and Cryopreservation of Mint Shoot Tips

Teixeira

González‐Benito

García

2013

Biotechnology Progress

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Section: Measurement Of Ice Heat Of Fusion Using Dscmentioning

confidence: 99%

Glassy State and Cryopreservation of Mint Shoot Tips

Teixeira

González‐Benito

García

2013

Biotechnology Progress

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“…Alternatively, EnvZ may respond to a collective property of the periplasmic compartment or cytoplasmic environment (i.e. macromolecular crowding or changes in water reactivity) (reviewed in Wiggins 1990).…”

Section: Activation Signalsmentioning

confidence: 99%

Signal transduction via the histidyl‐aspartyl phosphorelay

1997

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The histidyl-aspartyl phosphorelay, formerly described as the two-component system, is the predominant mode of signal transduction in bacteria. Adaptation to environmental changes occurs through a sensor histidine protein kinase and a response regulator. The histidine protein kinase is usually a transmembrane receptor and the response regulator is a cytoplasmic protein.Together the histidyl-aspartyl phosphorelay proteins mediate reversible phosphorylation events that control downstream effectors. Following autophosphorylation at a conserved histidine residue, the histidine kinase serves as a phospho-donor for the response regulator. Once phosphorylated, the response regulator mediates changes in gene expression or cellular locomotion. The EnvZ-OmpR phosphorelay system in Escherichia coli, which monitors external osmolarity and responds by differentially modulating the expression of the OmpF and OmpC major outer membrane porins, will be described as a model system. While histidine kinases were thought to be present only in prokaryotes, they have recently been identified in eukaryotic systems. Here, we review the unique and conserved features of this growing family of signal transducers.

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“…Biochemical adaptations fo environmental stresses offen involve fhe cellular accumulation of low-molecular-weighf organic solutes (protectants). If is now recognized that whereas pofassium is mainly associated with the negatively charged groups of macromolecules, osmoprofectants are mainly located in the free cyfoplasmic water (Wiggins, 1990;Cayley etai, 1991;1992). Cayley etai (1992) concluded that because fhe amounts of glycine befaine, proline and glufamate which were determined by using NMR specfroscopy of E. co//cell suspensions or by using chemical analyses, were the same, these osmolytes cannot be tightly bound to proteins in living cells.…”

Section: Protective Properties Of Trehalose and Other Solutesmentioning

confidence: 99%

Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression

Strøm

Kaasen

1993

Molecular Microbiology

340

240

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SummaryEndogenously synthesized trehalose is a stress protectant in Escherichia coli. Externally supplied trehalose does not serve as a stress protectant, but it can be utilized as the sole source of carbon and energy. Mutants defective in trehalose synthesis display an impaired osmotic tolerance in minimal growth media without glycine betaine, and an impaired stationary-phase-induced heat tolerance. Mechanisms for stress protection by trehalose are discussed. The genes for trehalose-6-phosphate synthase {otsA) and anabolic trehalose-6-phosphate phosphatase {otsB) constitute an operon. Their expression is induced both by osmotic stress and by growth into the stationary phase and depend on the sigma factor encoded by rpoS {katF). rpoS is amber-mutated in E. coti K-12 and its DNA sequence varies among K-12 strains. For trehalose catabolism under osmotic stress E. coli depends on the osmotically inducible periplasmic trehalase (TreA). In the absence of osmotic stress, trehalose induces the formation of an enzyme W^'^ (TreB) of the group translocation system, a catabolic trehalose-6-phosphate phosphatase (TreE), and an amylotrehalase (TreC) which converts trehalose to free glucose and a glucose polymer.

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Role of water in some biological processes.

Cited by 188 publications

References 68 publications

Glassy State and Cryopreservation of Mint Shoot Tips

Glassy State and Cryopreservation of Mint Shoot Tips

Signal transduction via the histidyl‐aspartyl phosphorelay

Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression

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