Literature DB >> 25784054

The Clothes Make the mRNA: Past and Present Trends in mRNP Fashion.

Guramrit Singh1, Gabriel Pratt, Gene W Yeo, Melissa J Moore.   

Abstract

Throughout their lifetimes, messenger RNAs (mRNAs) associate with proteins to form ribonucleoproteins (mRNPs). Since the discovery of the first mRNP component more than 40 years ago, what is known as the mRNA interactome now comprises >1,000 proteins. These proteins bind mRNAs in myriad ways with varying affinities and stoichiometries, with many assembling onto nascent RNAs in a highly ordered process during transcription and precursor mRNA (pre-mRNA) processing. The nonrandom distribution of major mRNP proteins observed in transcriptome-wide studies leads us to propose that mRNPs are organized into three major domains loosely corresponding to 5' untranslated regions (UTRs), open reading frames, and 3' UTRs. Moving from the nucleus to the cytoplasm, mRNPs undergo extensive remodeling as they are first acted upon by the nuclear pore complex and then by the ribosome. When not being actively translated, cytoplasmic mRNPs can assemble into large multi-mRNP assemblies or be permanently disassembled and degraded. In this review, we aim to give the reader a thorough understanding of past and current eukaryotic mRNP research.

Entities:  

Keywords:  RNA granules; RNA processing; RNP remodeling; coupling; mRNP packaging; ribonucleoproteins

Mesh:

Substances:

Year:  2015        PMID: 25784054      PMCID: PMC4804868          DOI: 10.1146/annurev-biochem-080111-092106

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  144 in total

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Journal:  Cell Rep       Date:  2013-12-19       Impact factor: 9.423

Review 4.  To the pore and through the pore: a story of mRNA export kinetics.

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Journal:  Biochim Biophys Acta       Date:  2012-02-22

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Journal:  Mol Cell       Date:  2012-06-08       Impact factor: 17.970

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Journal:  Cell       Date:  2012-05-31       Impact factor: 41.582

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8.  Structural basis for the assembly and disassembly of mRNA nuclear export complexes.

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Journal:  Biochim Biophys Acta       Date:  2012-03-02

9.  Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA.

Authors:  Jeffrey E Squires; Hardip R Patel; Marco Nousch; Tennille Sibbritt; David T Humphreys; Brian J Parker; Catherine M Suter; Thomas Preiss
Journal:  Nucleic Acids Res       Date:  2012-02-16       Impact factor: 16.971

10.  The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement.

Authors:  Thomas Sweet; Carrie Kovalak; Jeff Coller
Journal:  PLoS Biol       Date:  2012-06-12       Impact factor: 8.029

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Review 3.  Nonsense-mediated mRNA decay: The challenge of telling right from wrong in a complex transcriptome.

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7.  Rbfox Proteins Regulate Splicing as Part of a Large Multiprotein Complex LASR.

Authors:  Andrey Damianov; Yi Ying; Chia-Ho Lin; Ji-Ann Lee; Diana Tran; Ajay A Vashisht; Emad Bahrami-Samani; Yi Xing; Kelsey C Martin; James A Wohlschlegel; Douglas L Black
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Review 8.  Teaching an Old Virus New Tricks: A Review on New Approaches to Study Age-Old Questions in Influenza Biology.

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10.  The Evolutionarily-conserved Polyadenosine RNA Binding Protein, Nab2, Cooperates with Splicing Machinery to Regulate the Fate of pre-mRNA.

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