Inactivation of mRNA cap-binding protein complex in Drosophila melanogaster embryos under heat shock.

@article{Zapata1991InactivationOM,
  title={Inactivation of mRNA cap-binding protein complex in Drosophila melanogaster embryos under heat shock.},
  author={Juan Manuel Zapata and Federico Garc{\'i}a Maroto and Jos{\'e} Manuel Sierra},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 24},
  pages={
          16007-14
        }
}
View on PubMed
doi.org
53 Citations
Highly Influential Citations
1
Background Citations
11
Results Citations
2

53 Citations

Citation Type

Citation Type

Translational Regulation of Hsp90 mRNA
TLDR
The ability of Hsp90 mRNA to be preferentially translated is conferred by its 5′-UTR, but, in contrast to Hsp22 and -70, is primarily influenced by nucleotides close to the AUG initiation codon.
m7GpppG cap dependence for efficient translation of Drosophila 70-kDa heat-shock-protein (Hsp70) mRNA.
TLDR
Complementary experiments in which eIF-4 was inactivated in vitro using either m7GTP cap analogue or foot-and-mouth-disease virus L protease expression indicated that the cap-dependent translation pathway is required for optimal Hsp mRNA translation.
Translational control during heat shock.
Cap-independent translation of heat shock messenger RNAs.
TLDR
It has now become apparent that there are numerous similarities between translation in heat-shocked cells and translation in picornavirus-infected cells and other cells which predominately carry out cap-independent translation.
Efficient translation of an SSA1-derived heat-shock mRNA in yeast cells limited for cap-binding protein and eIF-4F
TLDR
It is reported here that decreased global translation initiation in cdc33 mutant cells has virtually no effect on the translation of mRNA from the SSA1 -lacZ chimeric gene, comprised of yeast SSA 1 hsp70 gene transcription and translation initiation sequences fused in-frame to the bacterial lacZ gene.
Heat Shock Increases the Association of Binding Protein-1 with Initiation Factor 4E*
TLDR
Examining the effects of heat shock on the regulation of the cap-binding initiation factor 4E and its inhibitory binding protein, 4E-BP1, in Chinese hamster ovary cells and in cardiac myocytes suggested that heat shock could provide a mechanism for the selective up-regulation of the synthesis of heatshock proteins and other stress proteins during heat shock.
Translational regulation of the heat shock response
TLDR
The emerging picture is that the two key steps of polypeptide chain initiation, namely mRNA binding and Met-tRNAi binding to ribosomes, are regulated in heat-shocked mammalian cells.
Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation
TLDR
It is shown that heat shock inhibits translation of capped mRNAs by simultaneously inducing dephosphorylation of eIF-4E and BP-1, suggesting that cells might coordinately regulate translation of cap-dependent mRN as well as finely regulate the efficiency of translation initiation or possibly control cap- dependent translation for fundamentally different purposes.
Striking multiplicity of eIF4E-BP1 phosphorylated isoforms identified by 2D gel electrophoresis regulation by heat shock.
TLDR
A complex set of eIF4E-BP1 phosphorylation isoforms is identified; changes in the expression of these isoforms in response to stresses such as heat shock may contribute to translation repression.
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.
...
...