In:
European Journal of Biochemistry, Wiley, Vol. 223, No. 3 ( 1994-08), p. 791-797
Kurzfassung:
Low amounts of Semliki Forest virus capsid protein transferred into target cells by electroporation‐mediated delivery (10 3 –10 4 molecules incorporated/cell) confer thermal resistance resulting in enhanced survival. Furthermore, when exposed to 43°C, these cells display an enhanced expression of heat‐shock protein‐70 and a translational thermotolerance. Similarly, low amounts of capsid protein transferred into cells in which transcription is blocked by actinomycin D, also protect the translation machinery at 43°C. In a cell‐free translation system, added capsid protein appears to modulate translational efficiency of endogenous mRNSs. At approximately 1 molecule/ribosome, capsid protein is able to enhance translation at 30°C and at 43°C. In contrast, high concentrations of capsid protein are responsible for a marked inhibition of protein synthesis at 30°C, but only hamper translational thermotolerance at 43°C. Our results favor the hypothesis that small amounts of capsid protein trigger a chaperone‐like activity that is able to protect the translational machinery from thermal damage.
Materialart:
Online-Ressource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1994.223.issue-3
DOI:
10.1111/j.1432-1033.1994.tb19054.x
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
1994
ZDB Id:
1398347-7
ZDB Id:
2172518-4
SSG:
12
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