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Zhan, M. et al. Transcriptional repression of protein kinase Cα via Sp1 by wild type p53 is involved in inhibition of multidrug resistance 1 P-glycoprotein phosphorylation.
These miRNAs can bind complementary to messenger RNA (mRNA) and lead to a repression of protein synthesis through degradation of mRNA or transcription blockade.
The genes encoding protein synthesis-related proteins such as aminoacyl-tRNA synthetase (Os03t0749300, Os05t0150900) translation initiation factor 2 (Os03t0296400) and translation elongation factor EF1B (Os06t0571400) were downregulated, suggesting a repression of protein turnover and recycling of amino acids in roots and shoots.
This results in increased p27 or LATS2 protein levels because DND1 inhibits miRNA-mediated repression of protein expression.
This results in translational repression of protein synthesis and, in some cases, destabilization of messenger RNA [1].
In addition, our results predict a global repression of protein translation within the cell due to the downregulation of multiple translation initiation factors.
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MicroRNAs (miRNAs) are a large family of single-stranded non-coding RNAs that direct the post-transcriptional repression of protein-coding genes in metazoans.
Although recent studies demonstrate that repression of proteins is frequently mirrored by decreased transcript levels of miRNA targets [15] [17], examples where translational repression is the major component of silencing have been identified as well [17] [19].
In addition to protecting the genome integrity, H3K9 trimethylation is also important for the transcriptional repression of protein-coding genes.
Overall, these results showed a general repression of proteins involved in the response to generic stress and a return to steady-state levels of those proteins specifically required for defence against pathogens.
We show that the expression of the EIF4EBP3 translational repressor represents a peripheral marker of CDC73 function and propose a model whereby starvation resistance, mediated at least in part by de-repression of protein translation, may contribute to parathyroid malignant transformation.
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