Interferon (IFN) is not able to induce heat-shock protein (HSP) synthesis. However IFN pretreatment of mouse L cells has been shown to enhance the decrease of overall protein synthesis which follows a heat shock, and to stimulate the accumulation of HSPs. We show here that the synthesis of a protein
Regulation of translation in rabbit reticulocytes and mouse L-cells; comparison of the effects of temperature
β Scribed by Nessly Craig
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 715 KB
- Volume
- 87
- Category
- Article
- ISSN
- 0021-9541
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β¦ Synopsis
Abstract
Various parameters of protein synthesis were analyzed in rabbit reticulocytes exposed to various temperatures for up to five hours. Between 10Β°C and 40Β°C total protein synthesis exhibited two different apparent activation energies (36 kcal/mole, 10β24Β°C; 22 kcal/mole, 24β40Β°C), as did protein elongation and release (35 kcal/mole, 10β25Β°C; 12 kcal/mole, 25β40Β°C). However, the level of polysomes remained essentially unchanged between 0Β°C and 42Β°C which implies that the activation energy for polypeptide initiation is quite similar to that for elongation and is also biphasic. This situation is different from that in cultured mouse Lβcells where the polysome level is dependent on temperatures. Nevertheless, reticulocytes and Lβcells appear to be similar in their temperature dependence of initiation and in their rate of elongation (5β6 amino acids/second at 36Β°C).
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