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A novel translational control mechanism involving RNA structures within coding sequences.

Jennifer Jungfleisch1, Danny D Nedialkova2,3, Ivan Dotu4

  • 1Molecular Virology Group, Department of Experimental and Health Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain.

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|November 9, 2016
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This study reveals how RNA structures in messenger RNA coding sequences are controlled by the DEAD-box helicase Dhh1, impacting protein production, especially for membrane proteins.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Translational Control

Background:

  • The role of RNA structures within coding sequences (CDS) of messenger RNAs (mRNAs) in regulating gene expression is not well understood.
  • Translational control mechanisms are crucial for cellular function and protein synthesis.

Purpose of the Study:

  • To identify and characterize a novel, conserved mechanism of translational control involving RNA structures in CDS and the DEAD-box helicase Dhh1.
  • To investigate the prevalence of this mechanism in viral and cellular mRNAs, particularly those encoding membrane and secreted proteins.

Main Methods:

  • Yeast genetics and genome-wide ribosome profiling analyses were employed.
  • Comparative analysis of viral and cellular mRNAs with specific focus on Dhh1-dependent transcripts.
  • Experimental approaches to investigate Dhh1 binding and activation of translation initiation.

Main Results:

  • A conserved mechanism of translational control mediated by RNA structures in CDS and Dhh1 was identified.
  • This mechanism applies to viral, yeast, and human mRNAs, especially those encoding membrane and secreted proteins.
  • Dhh1-dependent mRNAs share features like long, structured CDSs and specific Dhh1 binding, suggesting activation at the translation initiation step.

Conclusions:

  • RNA structures within CDS, in conjunction with RNA helicases like Dhh1, represent a novel layer of translational control.
  • Dhh1 plays a critical role in regulating the translation of specific mRNA subsets, including those for membrane and secretome proteins.
  • This discovery offers new avenues for understanding and manipulating the regulation of membrane and secreted protein synthesis.