Chapter 9 : Effects of Growth-Permissive Pressures on the Physiology of

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This chapter discusses the recent advances in explorations of the effects of growth-permissive pressures on the growth and physiology of . The simplest and most convenient system for high-pressure cultivation of is a pressure syringe, generally made of stainless steel or titanium, with a diameter of approximately 10 cm, length of 30 cm, and internal volume of about 500 ml, which can typically be used at pressures up to 200 MPa. Tryptophan uptake in is mediated by high-affinity-type tryptophan permease Tat2 and low-affinity-type tryptophan permease Tat1. The high-pressure-growth (HPG) mutants are classified into four semidominant linkage groups designated HPG1, HPG2, HPG3, and HPG4. It is worthwhile to examine the isolation of HPG mutants from nutrient-prototrophic strains. Hydrostatic pressure causes intracellular acidification in a manner analogous to that of weak acid treatment. Therefore, intracellular acidification may cause HSP30 induction with hydrostatic pressure. Organic osmolytes such as amino acids and their derivatives, polyols, sugars, and methylamines are used by the cells of water-stressed organisms to maintain cell volume. By exploiting genomic information and powerful tools for genetic manipulation, the effects of hydrostatic pressure on have been analyzed by investigators in a broad range of experimental fields, including physiology, biochemistry, molecular biology, and food sciences. Using hydrostatic pressure as a parameter, piezophysiology can uncover novel biological phenomena that are accompanied by large volume changes, not only in but also in many other organisms.

Citation: Abe F. 2008. Effects of Growth-Permissive Pressures on the Physiology of , p 167-179. In Michiels C, Bartlett D, Aersten A (ed), High-Pressure Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555815646.ch9
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Image of Figure 1.
Figure 1.

Model depicting the regulation of the high-affinity tryptophan permease Tat2 in response to high pressure. Upon incubation of the wild-type cells at high pressure, Tat2 is assumed to be partially denatured with retention of some activity. Then, the denatured Tat2 is recognized by the ubiquitin system, followed by degradation in the vacuoles or by the proteasomes. Upon the loss of any factors involved in the degradation pathway, Tat2 is stabilized in the plasma membrane. Consequently, the mutant cells become endowed with the ability to grow at high pressure. Ub, ubiquitin; K, lysine residue(s); Rsp5, ubiquitin ligase Rsp5; Bul1/2, binding proteins of Rsp5; Doa4, Ubp6, Ubp14, ubiquitin-specific proteases; MVB, multivesicular body; Vps27, an endosomal protein that functions at the MVB.

Citation: Abe F. 2008. Effects of Growth-Permissive Pressures on the Physiology of , p 167-179. In Michiels C, Bartlett D, Aersten A (ed), High-Pressure Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555815646.ch9
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Image of Figure 2.
Figure 2.

Model depicting the dynamics of tryptophan import through Tat1 and Tat2. Tat1 is associated with lipid rafts, whereas Tat2 is localized in nonrafts. The large activation volumes (Δ ) for Tat1- and Tat2-mediated tryptophan import are accounted for mainly by volume changes associated with protein conformational changes. The initial volume of Tat1 is smaller than that of Tat2 because Tat1 is localized in the highly ordered lipid microdomain of lipid rafts. the volume of the permease in the initial state; , the volume of the permease in the activated state; Δ , the activation volume accompanied by tryptophan import through the permease.

Citation: Abe F. 2008. Effects of Growth-Permissive Pressures on the Physiology of , p 167-179. In Michiels C, Bartlett D, Aersten A (ed), High-Pressure Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555815646.ch9
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Generic image for table
Table 1.

Effects of growth-permissive pressure on the growth and physiology of

Citation: Abe F. 2008. Effects of Growth-Permissive Pressures on the Physiology of , p 167-179. In Michiels C, Bartlett D, Aersten A (ed), High-Pressure Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555815646.ch9

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