m7GpppG cap dependence for efficient translation of Drosophila 70-kDa heat-shock-protein (Hsp70) mRNA.

@article{Song1995m7GpppGCD,
  title={m7GpppG cap dependence for efficient translation of Drosophila 70-kDa heat-shock-protein (Hsp70) mRNA.},
  author={H. J. Song and Daniel R Gallie and Roger F. Duncan},
  journal={European journal of biochemistry},
  year={1995},
  volume={232 3},
  pages={
          778-88
        }
}
To investigate whether preferential translation of the heat-shock mRNAs occurs via cap-independent translation, the requirement for the m7GpppG cap structure for efficient translation of 70-kDa heat-shock-protein (Hsp70) mRNA was quantified by in vitro translation and by in vivo translation following electroporation. Hsp70 mRNA was transcribed in vitro with and without a cap structure. Translation in the rabbit reticulocyte or wheat germ lysate was reduced about 70% when the cap was absent. For… 
Cap-independent translation of maize Hsp101.
TLDR
Data suggest that the 5'UTR of maize Hsp101, a plant cellular mRNA, functions as an IRES-like element accounting for its cap-independent translation during heat stress.
Sequence and structure determinants of Drosophila Hsp70 mRNA translation: 5'UTR secondary structure specifically inhibits heat shock protein mRNA translation.
TLDR
Results indicate that heat shock reduces the capacity to unwind 5-UTR secondary structure, allowing only mRNAs with minimal 5'-UTRsecondary structure to be efficiently translated.
Rapamycin conditionally inhibits Hsp90 but not Hsp70 mRNA translation in Drosophila: implications for the mechanisms of Hsp mRNA translation
  • R. Duncan
  • Biology, Computer Science
    Cell Stress and Chaperones
  • 2008
TLDR
Results show that rapamycin strongly inhibits global translation in Drosophila cells, and support the proposal that preferential translation of different Hsp mRNA utilizes distinct translation mechanisms, even within a single species.
Cleavage of Eukaryotic Translation Initiation Factor 4G by Exogenously Added Hybrid Proteins Containing Poliovirus 2Apro in HeLa Cells: Effects on Gene Expression
TLDR
Findings indicate that intact eIF4G is necessary for the translation of mRNAs not engaged in translation with the exception of heat shock m RNAs but is not necessary forThe translation ofmRNAs that are being translated.
Turnover and Translation of in Vitro Synthesized Messenger RNAs in Transfected, Normal Cells*
TLDR
These data demonstrate the presence of 3′-UTR, destabilizing, and translational regulatory elements outside of the AUUUA repeats and unambiguously show that actinomycin D at concentrations commonly used to inhibit transcription stabilizes cytokine mRNAs.
Errors in macromolecular synthesis after stress. A study of the possible protective role of the small heat shock proteinsBiochemistry
TLDR
There is molecular misreading of sequence repeats and that this misreading is induced by stress, and a relaxed stringency of AUG selection induced by heat shock is described.
Alteration of HSF3 and HSP70 mRNA expression in the tissues of two chicken breeds during acute heat stress.
TLDR
The results indicate that the expression of HSF3 and HSP70 mRNA in LSC and WRR exhibit species-specific and tissue-specific differences during heat treatment.
...
...

References

SHOWING 1-10 OF 63 REFERENCES
Dependence of the adenovirus tripartite leader on the p220 subunit of eukaryotic initiation factor 4F during in vitro translation. Effect of p220 cleavage by foot-and-mouth-disease-virus L-protease on in vitro translation.
TLDR
In vitro protein-synthesis experiments with purified initiation factors confirmed the dependence of TPT mRNA translation on eukaryotic initiation factor 4F, and the relationship between adenovirus TPT-5'UTR-directed translation and poliovirus-induced host cell shut-off is discussed.
Heat shock effects on phosphorylation of protein synthesis initiation factor proteins eIF-4E and eIF-2 alpha in Drosophila.
TLDR
A major phosphoprotein which copurifies with eIF-4E on m7GTP-Sepharose shows decreased overall phosphorylation and decreased association with eif- 4E following heat shock, which suggests it is Drosophila e IF-4B.
Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation.
TLDR
In vitro assays for initiation factor activities reveal heat shock inhibits eukaryotic initiation factor 2 (eIF-2), eIF-(3 + 4F), and eIF-4B, while enzymatic activities induced by heat shock inhibit protein synthesis and modify initiation factors in a rabbit reticulocyte lysate.
...
...