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. 1988 Oct;54(10):2375–2380. doi: 10.1128/aem.54.10.2375-2380.1988

Pressure-Induced Alterations in the Protein Pattern of the Thermophilic Archaebacterium Methanococcus thermolithotrophicus

R Jaenicke 1,*, G Bernhardt 1, H-D Lüdemann 1, K O Stetter 1
PMCID: PMC204265  PMID: 16347748

Abstract

Elevated hydrostatic pressure has been shown to affect the growth rate of the thermophilic methanobacterium Methanococcus thermolithotrophicus without extending its temperature range of viability. Analysis of the cell inventory after ≈ 10 h of incubation at 65°C and 50 MPa (applying high-pressure liquid chromatography and two-dimensional gel electrophoresis) proved that pressure induces alterations in the protein pattern and the amino acid composition of the total cell hydrolysate. Gels showed that after pressurization a series of (basic) proteins with a molecular mass in the range of 38 and 70 kilodaltons occurs which is not detectable in cells grown at normal atmospheric pressure. The question of whether the observed alterations are caused by the perturbation of the balance of protein synthesis and turnover or by the pressure-induced synthesis of compounds analogous to heat shock proteins remains unanswered.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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