TOP mRNPs: Molecular Mechanisms and Principles of Regulation

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, whi...

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Main Authors: Eric Cockman, Paul Anderson, Pavel Ivanov
Format: Article
Language:English
Published: MDPI AG 2020-06-01
Series:Biomolecules
Subjects:
RNA
Online Access:https://www.mdpi.com/2218-273X/10/7/969
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spelling doaj-06bf8a1450a3421b9dd8991f81869e9c2020-11-25T03:19:22ZengMDPI AGBiomolecules2218-273X2020-06-011096996910.3390/biom10070969TOP mRNPs: Molecular Mechanisms and Principles of RegulationEric Cockman0Paul Anderson1Pavel Ivanov2Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115, USABrigham and Women’s Hospital, Harvard Medical School, Harvard Initiative for RNA Medicine, Boston, MA 02115, USABrigham and Women’s Hospital, Harvard Medical School, Harvard Initiative for RNA Medicine, Boston, MA 02115, USAThe 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.https://www.mdpi.com/2218-273X/10/7/9695’ Terminal OligopyrimidineRNA binding proteinsLARP1translation regulationRNA
collection DOAJ
language English
format Article
sources DOAJ
author Eric Cockman
Paul Anderson
Pavel Ivanov
spellingShingle Eric Cockman
Paul Anderson
Pavel Ivanov
TOP mRNPs: Molecular Mechanisms and Principles of Regulation
Biomolecules
5’ Terminal Oligopyrimidine
RNA binding proteins
LARP1
translation regulation
RNA
author_facet Eric Cockman
Paul Anderson
Pavel Ivanov
author_sort Eric Cockman
title TOP mRNPs: Molecular Mechanisms and Principles of Regulation
title_short TOP mRNPs: Molecular Mechanisms and Principles of Regulation
title_full TOP mRNPs: Molecular Mechanisms and Principles of Regulation
title_fullStr TOP mRNPs: Molecular Mechanisms and Principles of Regulation
title_full_unstemmed TOP mRNPs: Molecular Mechanisms and Principles of Regulation
title_sort top mrnps: molecular mechanisms and principles of regulation
publisher MDPI AG
series Biomolecules
issn 2218-273X
publishDate 2020-06-01
description 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.
topic 5’ Terminal Oligopyrimidine
RNA binding proteins
LARP1
translation regulation
RNA
url https://www.mdpi.com/2218-273X/10/7/969
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AT paulanderson topmrnpsmolecularmechanismsandprinciplesofregulation
AT pavelivanov topmrnpsmolecularmechanismsandprinciplesofregulation
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