Low temperatures stabilize interferon ?-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli

Chesshyre, Julian A.; Hipkiss, Alan R.

doi:10.1007/bf00262455

Cited by 67 publications

(25 citation statements)

References 16 publications

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“…For example, interferon a-2 is rapidly degraded at 37 "C in E. coli and Methylophilus methylotrophus, but is stable in both organisms at 29°C and below (Chesshyre & Hipkiss, 1989). Other polypeptides of interest might undergo similar stabilization, but at much lower temperatures.…”

Section: Discussionmentioning

confidence: 99%

Temperature-dependent changes in proteolytic activities and protein composition in the psychrotrophic bacterium Arthrobacter globiformis S155

Potier

Drevet

Gounot

et al. 1990

Journal of General Microbiology

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Proteolytic activities, active against casein and insulin are present in cell-free extracts of the psychrotrophic bacterium Arthrobuctergkbb@iormis s155. These activities were compared (i) following growth of the bacterium at different temperatures (10, 20 and 32 "C) and (ii) after a temperature shift from 10 to 32 "C. Both activities (measured at 20 "C) were greater in cells grown at 32 "C and after a temperature shift. Chloramphenicol prevented the increases in activities. The proteolysis of casein was stimulated by ATP; the stimulation was greater following a temperature shift. In addition, proteolysis of casein (measured at 20°C) was activated by pre-incubation at temperatures between 45 and 60°C; the proportion of proteolytic activity activated by such treatment also increased with growth temperature. Comparison by two-dimensional electrophoresis of the polypeptides synthesized at 10 and 32 "C suggests that A. gbbvormis S155 produces proteins specific to both temperatures (13 species were either exclusive to or present in increased amounts during growth at 1O"C, while at least 21 polypeptides were preferentially synthesized at 32°C). A temperature shift from 10 to 32°C promoted the synthesis of at least 16 polypeptides, many with M, values similar to those of heat shock proteins synthesized at higher temperatures in mesophiles. A temperature up-shift of A. globiformis S155 from 10 to 20 "C did not provoke the synthesis of new proteins; heat shock proteins were produced only at 28 "C and higher. The similarity in kinetics of the appearance of heat shock proteins and the increase in proteolytic activities suggest that in A. gkbbvormis S155 some heat shock proteins might also possess protein catabolic function.

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Section: Discussionmentioning

confidence: 99%

Temperature-dependent changes in proteolytic activities and protein composition in the psychrotrophic bacterium Arthrobacter globiformis S155

Potier

Drevet

Gounot

et al. 1990

Journal of General Microbiology

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“…On the other hand, the activity and expression of a number of E. coli chaperones are increased at lower growth temperatures. It has also been observed that temperature reduction leads to the low activity of heat shock proteases which are induced during over-expression [5,9,15]. In addition to temperature shifts, the heat-shock response has also been induced by a variety of stress conditions, for example harmful substances such as ethanol [16].…”

Section: Introductionmentioning

confidence: 98%

Optimizing conditions for production of high levels of soluble recombinant human growth hormone using Taguchi method

Savari

Zarkesh-Esfahani

Edalati

et al. 2015

Protein Expression and Purification

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“…Thus, even though protease III is dispensable for E. coli growth, it may play an important physiological role in cells grown in certain environments. Chesshyre and Hipkiss (1989) showed that the turnover rate of aberrant polypeptides was reduced by about 40% when E. coli and Methylophilus methylotrophus were grown at 25 ° C instead of 37 ° C. They also demonstrated that interferon a-2 was stabilized at 25°C in both organisms. The increased degradation at temperatures greater than 30°C was attributed to conformational changes in the polypeptide, which result in the exposure of protease cleavage sites.…”

Section: Effect Of Culture P Hmentioning

confidence: 85%

Optimization of growth conditions for the production of proteolytically-sensitive proteins in the periplasmic space of Escherichia coli

Baneyx

Ayling

Palumbo

et al. 1991

Appl Microbiol Biotechnol

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The expression of many secreted recombinant proteins in Gram-negative bacteria is limited by degradation in the periplasmic space. We have previously shown that the production of protein A-beta-lactamase, a secreted fusion protein highly sensitive to proteolysis in Escherichia coli, can be increased in mutant strains deficient in up to three cell-envelope-associated proteolytic activities. In this work we investigated the effect of fermentation conditions on suppressing any residual proteolytic activity in various protease-deficient strains. Optimal production of the fusion protein was observed in cells grown under mildly acidic conditions (5.5 less than or equal to pH less than or equal to 6.0) and a low temperatures. These conditions were shown to specifically decrease the rate of proteolysis. In addition, a further increase in production was observed in cultures supplemented with 0.5 to 0.75 mM zinc chloride. This may relate to the inhibition of a cell envelope protease by Zn2+ ions.

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Low temperatures stabilize interferon ?-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli

Cited by 67 publications

References 16 publications

Temperature-dependent changes in proteolytic activities and protein composition in the psychrotrophic bacterium Arthrobacter globiformis S155

Temperature-dependent changes in proteolytic activities and protein composition in the psychrotrophic bacterium Arthrobacter globiformis S155

Optimizing conditions for production of high levels of soluble recombinant human growth hormone using Taguchi method

Optimization of growth conditions for the production of proteolytically-sensitive proteins in the periplasmic space of Escherichia coli

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