ISSN:
1573-4978
Schlagwort(e):
Drosophila
;
eIF-2
;
eIF-4F
;
heat shock
;
mRNA translation regulation
;
phosphorylation
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Abstract All organisms from bacteria to man respond to an exposure to higher than physiological temperatures by reprogramming their gene expression, leading to the increased synthesis of a unique set of proteins termed heat shock proteins (hsps). The hsps function as molecular chaperones in both normal and stressed cells. The rapid and efficient synthesis of hsps is achieved as a result of changes occurring at gene transcription, RNA processing and degradation, and mRNA translation. With regard to the translational regulation, the emerging picture is that the two key steps of polypeptide chain initiation, namely mRNA binding and Met-tRNA i binding to ribosomes, are regulated in heat-shocked mammalian cells. InDrosophila, mRNA binding is regulated by a structural feature of the leader of heat shock mRNAs and by the inactivation of eukaryotic initiation factor- (eIF-) 4F. No clear evidence for changes in Met-tRNA i binding has been obtained yet.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00986963
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