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TOP mRNPs: Molecular Mechanisms and Principles of Regulation

1
Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115, USA
2
Brigham and Women’s Hospital, Harvard Medical School, Harvard Initiative for RNA Medicine, Boston, MA 02115, USA
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(7), 969; https://doi.org/10.3390/biom10070969
Received: 21 May 2020 / Revised: 20 June 2020 / Accepted: 23 June 2020 / Published: 27 June 2020
(This article belongs to the Special Issue Ribonucleoprotein Particles (RNPs): From Structure to Function)
The cellular response to changes in the surrounding environment and to stress requires the coregulation of gene networks aiming to conserve energy and resources. This is often achieved by downregulating protein synthesis. The 5' Terminal OligoPyrimidine (5' TOP) motif-containing mRNAs, which encode proteins that are essential for protein synthesis, are the primary targets of translational control under stress. The TOP motif is a cis-regulatory RNA element that begins directly after the m7G cap structure and contains the hallmark invariant 5'-cytidine followed by an uninterrupted tract of 4–15 pyrimidines. Regulation of translation via the TOP motif coordinates global protein synthesis with simultaneous co-expression of the protein components required for ribosome biogenesis. In this review, we discuss architecture of TOP mRNA-containing ribonucleoprotein complexes, the principles of their assembly, and the modes of regulation of TOP mRNA translation.
Keywords: 5’ Terminal Oligopyrimidine; RNA binding proteins; LARP1; translation regulation; RNA 5’ Terminal Oligopyrimidine; RNA binding proteins; LARP1; translation regulation; RNA
MDPI and ACS Style

Cockman, E.; Anderson, P.; Ivanov, P. TOP mRNPs: Molecular Mechanisms and Principles of Regulation. Biomolecules 2020, 10, 969.

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