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

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in

Effects of Growth-Permissive Pressures on the Physiology of , Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555815646/9781555814236_Chap09-1.gif /docserver/preview/fulltext/10.1128/9781555815646/9781555814236_Chap09-2.gif


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

Key Concept Ranking

Amino Acids
Amino Acid Addition
Highlighted Text: Show | Hide
Loading full text...

Full text loading...


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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint


1. Abe, F. 1998. Hydrostatic pressure enhances vital staining with carboxyfluorescein or carboxydichlorofluorescein in Saccharomyces cerevisiae: efficient detection of labeled yeasts by flow cytometry. Appl. Environ. Microbiol. 64:11391142.
2. Abe, F. 2004. Piezophysiology of yeast: occurrence and significance. Cell. Mol. Biol. 50:437445.
3. Abe, F., and, K. Horikoshi. 1995. Hydrostatic pressure promotes the acidification of vacuoles in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 130:307312.
4. Abe, F., and, K. Horikoshi. 1997. Vacuolar acidification in Saccharomyces cerevisiae induced by elevated hydrostatic pressure is transient and is mediated by vacuolar H+-ATPase. Extremophiles 1:8993.
5. Abe, F., and, K. Horikoshi. 1998. Analysis of intracellular pH in the yeast Saccharomyces cerevisiae under elevated hydrostatic pressure: a study in baro-(piezo-) physiology. Extremophiles 2:223228.
6. Abe, F., and, K. Horikoshi. 2000. Tryptophan permease gene TAT2 confers high-pressure growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 20:80938102.
7. Abe, F., and, K. Horikoshi. 2000. Metabolic changes in glycolysis in yeast induced by elevated hydrostatic pressure. A study in baro-(piezo-)physiology, p. 335337. In M. H. Manghnani,, W. J. Nellis, and, M. F. Nicole (ed.), Science and Technology of High-Pressure Research. University Press, Hyderabad, India.
8. Abe, F., and, K. Horikoshi. 2001. The biotechnological potential of piezophiles. Trends Biotechnol. 19:102 108.
9. Abe, F., and, H. Iida. 2003. Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2. Mol. Cell. Biol. 23:75667584.
10. Abe, F.,, C. Kato, and, K. Horikoshi. 1999. Pressure-regulated metabolism in microorganisms. Trends Microbiol. 7:447452.
11. Amerik, A. Y.,, S. Swaminathan,, B. A. Krantz,, K. D. Wilkinson, and, M. Hochstrasser. 1997. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16:48264838.
12. Bartlett, D. H. 2002. Pressure effects on in vivo microbial processes. Biochim. Biophys. Acta 1595:367381.
13. Beck, T.,, A. Schmidt, and, M. N. Hall. 1999. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell Biol. 146:12271237.
14. Chasse, S. A., and, H. G. Dohlman. 2004. Identification of yeast pheromone pathway modulators by high-throughput agonist response profiling of a yeast gene knockout strain collection. Methods Enzymol. 389:399 409.
15. Chong, P. L.,, P. A. Fortes, and, D. M. Jameson. 1985. Mechanisms of inhibition of (Na, K)-ATPase by hydrostatic pressure studied with fluorescent probes. J. Biol. Chem. 260:1448414490.
16. Cossins, A. R., and, A. G. Macdonald. 1989. The adaptation of biological membranes to temperature and pressure: fish from the deep and cold. J. Bioenerg. Biomembr. 21:115135.
17. deSmedt, H.,, R. Borghgraef,, F. Ceuterick, and, K. Heremans. 1979. Pressure effects on lipid-protein interactions in (Na++K+)-ATPase. Biochim. Biophys. Acta 556:479489.
18. Dubaquie, Y.,, R. Looser, and, S. Rospert. 1997. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc. Natl. Acad. Sci. USA 94:90119016.
19. Dupré, S., and, R. Haguenauer-Tsapis. 2001. Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase. Mol. Cell. Biol. 21:44824494.
20. Fujii, S.,, H. Iwahashi,, K. Obuchi,, T. Fujii, and, Y. Komatsu. 1996. Characterization of a barotolerant mutant of the yeast Saccharomyces cerevisiae: importance of trehalose content and membrane fluidity. FEMS Microbiol. Lett. 141:97101.
21. Glover, J. R., and, S. Lindquist. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:7382.
22. Guterman, A., and, M. H. Glickman. 2004. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J. Biol. Chem. 279:17291738.
23. Hicke, L. 1999. Gettin’ down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9:107112.
24. Ichimori, H.,, T. Hata,, H. Matsuki, and, S. Kaneshina. 1998. Barotropic phase transitions and pressure-induced interdigitation on bilayer membranes of phospholipids with varying acyl chain lengths. Biochim. Biophys. Acta 1414:165174.
25. Iwahashi, H.,, S. C. Kaul,, K. Obuchi, and, Y. Komatsu. 1991. Induction of barotolerance by heat shock treatment in yeast. FEMS Microbiol. Lett. 80:325328.
26. Iwahashi, H.,, K. Obuchi,, S. Fujii, and, Y. Komatsu. 1997. Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae. FEBS Lett. 416:15.
27. Iwahashi, H.,, M. Odani,, E. Ishidou, and, E. Kitagawa. 2005. Adaptation of Saccharomyces cerevisiae to high hydrostatic pressure causing growth inhibition. FEBS Lett. 579:28472852.
28. Kakinuma, Y.,, Y. Ohsumi, and, Y. Anraku. 1981. Properties of H+-translocating adenosine triphosphatase in vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem. 256:1085910863.
29. Kato, C., and, D. H. Bartlett. 1997. The molecular biology of barophilic bacteria. Extremophiles 1:111116.
30. Kato, M.,, R. Hayashi,, T. Tsuda, and, K. Taniguchi. 2002. High pressure-induced changes of biological membrane. Study on the membrane-bound Na+/K+-ATPase as a model system. Eur. J. Biochem. 269:110118.
31. Katzmann, D. J.,, M. Babst, and, S. D. Emr. 2001. Ubiqutin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1. Cell 106:145155.
32. Kobori, H.,, M. Sato,, K. Tameike,, K. Hamada,, S. Shimada, and, M. Osumi. 1995. Ultrastructural effects of pressure stress to the nucleus in Saccharomyces cerevisiae: a study by immunoelectron microscopy using frozen thin sections. FEMS Microbiol. Lett. 132:253258.
33. Leonhardt, S. A.,, K. Fearson,, P. N. Danese, and, T. L. Mason. 1993. HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol. Cell. Biol. 13:63046313.
34. Macdonald, A. G. 1967. The effect of high hydrostatic pressure on the cell division and growth of Tetrahymena pyriformis. Exp. Cell Res. 47:569580.
35. Malki, A.,, T. Caldas,, J. Abdallah,, R. Kern,, V. Eckey,, S. J. Kim,, S. S. Cha,, H. Mori, and, G. Richarme. 2005. Peptidase activity of the Escherichia coli Hsp31 chaperone. J. Biol. Chem. 280:1442014426.
36. Marquis, R. E. 1976. High-pressure microbial physiology. Adv. Microb. Physiol. 14:159241.
37. Martin, A. C., and, D. G. Drubin. 2003. Impact of genome-wide functional analyses on cell biology research. Curr. Opin. Cell Biol. 15:613.
38. Mentre, P., and, G. HuiBonHoa. 2001. Effects of high hydrostatic pressure on living cells: a consequence of the properties of macromolecules and macromolecule-associated water. Int. Rev. Cytol. 201:184.
39. Miura, T., and, F. Abe. 2004. Multiple ubiquitin-specific protease genes are involved in degradation of yeast tryptophan permease Tat2 at high pressure. FEMS Microbiol. Lett. 239:171179.
40. Miura, T.,, H. Minegishi,, R. Usami, and, F. Abe. 2006. Systematic analysis of HSP gene expression and effects on cell growth and survival at high hydrostatic pressure in Saccharomyces cerevisiae. Extremophiles 10:279284.
41. Nagayama, A.,, C. Kato, and, F. Abe. 2004. The C-terminal mutation stabilizes the yeast tryptophan permease Tat2 under high-pressure and low-temperature conditions. Extremophiles 8:143149.
42. Nelson, C. M.,, M.R. Schuppenhauer, and, D. S. Clark. 1992. High-pressure, high-temperature bioreactor for comparing effects of hyperbaric and hydrostatic pressure on bacterial growth. Appl. Environ. Microbiol. 58:17891793.
43. Nikko, E.,, A. M. Marini, and, B. André. 2003. Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway. J. Biol. Chem. 278:5073250743.
44. Perrier-Cornet, J. M.,, P. A. Marechal, and, P. Gervais. 1995. A new design intended to relate high pressure treatment to yeast cell mass transfer. J. Biotechnol. 41:4958.
45. Piper, P. W.,, C. Ortiz-Calderon,, C. Holyoak,, P. Coote, and, M. Cole. 1997. Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H(+)-ATPase. Cell Stress Chaperones 2:1224.
46. Sato, M.,, H. Kobori,, S. A. Ishijima,, Z. H. Feng,, K. Hamada,, S. Shimada, and, M. Osumi. 1996. Schizosaccharomyces pombe is more sensitive to pressure stress than Saccharomyces cerevisiae. Cell Struct. Funct. 21:167174.
47. Schmidt, A.,, M. N. Hall, and, A. Koller. 1994. Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake. Mol. Cell. Biol. 14:65976606.
48. Serrano, R. 1993. Structure, function and regulation of plasma membrane H+-ATPase. FEBS Lett. 325:108111.
49. Seymour, I. J., and, P. W. Piper. 1999. Stress induction of HSP30, the plasma membrane heat shock protein gene of Saccharomyces cerevisiae, appears not to use known stress-regulated transcription factors. Microbiology 145:231239.
50. Simons, K., and, E. Ikonen. 1997. Functional rafts in cell membranes. Nature 387:569572.
51. Somero, G. N. 1992. Adaptations to high hydrostatic pressure. Annu. Rev. Physiol. 54:557577.
52. Swezey, R. R., and, G. N. Somero. 1985. Pressure effects on actin self-assembly: interspecific differences in equilibrium kinetics of the G to F transformation. Biochemistry 24:852860.
53. Tamura, K.,, Y. Kamiki, and, M. Miyashita. 1999. Measurement of microbial activities under high pressure by calorimetry, p. 4750. In H. Ludwig (ed.), Advances in High Pressure Bioscience and Biotechnology. Springer, Berlin, Germany.
54. Winter, R., and, W. Dzwolak. 2004. Temperature-pressure configurational landscape of lipid bilayers and proteins. Cell. Mol. Biol. 50:397417.
55. Yanagibayashi, M.,, Y. Nogi,, L. Li, and, C. Kato. 1999. Changes in the microbial community in Japan Trench sediment from a depth of 6292 m during cultivation without decompression. FEMS Microbiol. Lett. 170:271279.
56. Yancey, P. H.,, W. R. Blake, and, J. Conley. 2002. Unusual organic osmolytes in deep-sea animals: adaptation to hydrostatic pressure and other perturbations. Comp. Biochem. Physiol. A 133:667676.
57. Yayanos, A. A. 1995. Microbiology to 10,500 meters in the deep sea. Annu. Rev. Microbiol. 49:777805.
58. Zimmerman, A. M. 1971. High-pressure studies in cell biology. Int. Rev. Cytol. 30:147.


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

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error