|Pressure-induced proteins in a new barophilic and hyperthermophilic archaeon from a deep-sea hydrothermal vent, isolated under high hydrostatic pressure|
Marteinsson, V.T.; Birrien, J.L.; Reysenbach, A.-L.; Vernet, M.; Prieur, D. (1997). Pressure-induced proteins in a new barophilic and hyperthermophilic archaeon from a deep-sea hydrothermal vent, isolated under high hydrostatic pressure, in: Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2): pp. 133-134
In: (1997). Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2)[s.n.][s.l.]. 111-149 pp., more
In: Cahiers de Biologie Marine. Station Biologique de Roscoff: Paris. ISSN 0007-9723, more
|Authors|| || Top |
- Marteinsson, V.T.
- Birrien, J.L.
- Reysenbach, A.-L.
A novel, barophilic, hyperthermophilic and anaerobic sulphur metabolizing archaeon, Thermococcus barophilus, strain MP, was isolated from a hydrothermal vent site (Snakepit) on the Mid-Atlantic Ridge (depth 3500 m). Enrichments and isolation were done under 4OMPa hydrostatic pressure at 95 degree C. Strain MP is barophilic at 75, 80, 85, 90, 95 and 98 degree C and is an obligate barophile between 95 degree C up to IOOiC (Tmax). For growth above 95 degree C a pressure of between 15 to 17.5 MPa is required. The strains grow between 48 to 95 degree C under atmospheric pressure. The optimal temperature for growth is 85 degree C at both high (40MPa) and low (0.3 MPa) pressures. The growth rate is two-fold higher at 85 degree C under in situ hydrostatic pressure than at low pressure. The whole-cell protein composition of the strain cultivated under high and low pressure at 85 degree C, was examined by one-dimensional SDS gradient gel electrophoresis. Two pressure-related proteins, showing opposing induction responses were observed. One protein (P35), with a molecular mass of approximately 35.5 kDa, was prominent at 40 MPa hydrostatic pressure but not at 0.3 hydrostatic or 0.1 MPa atmospheric pressures. Another protein (P60), with a molecular mass of approximately 6OkDa, was induced at 0.3 hydrostatic and 0.1 MPa atmospheric pressures but not at 40 MPa. About 40 and 17 amino acids were sequenced from the N-terminal ends of the pressure induced and the decompressurized protein, respectively. No amino acids sequence homology was found in the Genbank data base for protein P35. However, P60 most closely resembled (81%) the heat shock protein HHSP from the hyperthermophile Desulfurococcus SY and (81%) the heat shock protein of Pyrococcus strain KODI.