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Wiley Interdisciplinary Reviews:
RNA
Volume 10 Issue 1 (January/February 2019)
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Maturation of pre‐40S particles in yeast and humans
Published Online: Nov 08 2018
DOI: 10.1002/wrna.1516
Production of the small ribosomal subunit in eukaryotes involves the co‐transcriptional assembly of an initial pre‐ribosomal particle containing a subset of ribosomal proteins (RPs) as well as assembly and maturation factors (AFs). This initial pre‐ribosomal particle is split into pre‐40S and pre‐60S pre‐ribosomal particles that follow independent maturation pathways. This review deals with pre‐40S particle maturation only. The nuclear pre‐40S particles are exported via the nuclear pores into the cytoplasm. There, the AFs that function in RP recruitment and control ribosomal RNA (rRNA) folding are sequentially removed. In addition, in yeast at least, cytoplasmic pre‐40S particles are submitted to a quality control process involving a transient interaction with a 60S ribosomal subunit. At the end of the maturation pathway, 18S rRNA is released by an endonucleolytic cleavage.
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Gaining insight into transcriptome‐wide RNA population dynamics through the chemistry of 4‐thiouridine
Published Online: Oct 28 2018
DOI: 10.1002/wrna.1513
Newly transcribed RNAs can be metabolically labeled with 4‐thiouridine (s4U) to study many aspects of RNA metabolism genome‐wide, including RNA turnover, transient transcription, and polymerase elongation. New RNAs can be detected via biochemical enrichment (top) or nucleoside recoding to induce U‐to‐C mutations in s4U‐RNA in high‐throughput sequencing.
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The complex enzymology of mRNA decapping: Enzymes of four classes cleave pyrophosphate bonds
Published Online: Oct 21 2018
DOI: 10.1002/wrna.1511
Enzymes that hydrolyse the 5′ end of RNAs belong to four different enzyme classes: Nudix hydrolases, histidine triad (HIT) proteins, DXO proteins, and ApaH‐like phosphatases.
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The dynamic RNA modification 5‐methylcytosine and its emerging role as an epitranscriptomic mark
Published Online: Oct 11 2018
DOI: 10.1002/wrna.1510
5‐methylcytosine is emerging as an important epitranscriptomic mark of RNA. Various RNA methyltransferases that reside at different locations in the cell install this mark on a variety of RNA types. These range from cytoplasmic and mitochondrial rRNA and tRNA to mRNA and to various other non‐coding RNAs. Similar to the mulitude of targets, many if not most aspects of RNA metabolism may be affected by the m5C mark.
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Contributions of regulated transcription and mRNA decay to the dynamics of gene expression
Published Online: Oct 01 2018
DOI: 10.1002/wrna.1508
Transcriptional factors (TFs) regulate mRNA synthesis whereas RNA‐binding proteins (RBPs) regulate mRNA fate, such as stability. Various genome‐wide approaches provide the information for analyzing the function of the gene expression regulators. From these genome‐wide data, computational analysis constructs gene regulatory networks.
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Toxins targeting transfer RNAs: Translation inhibition by bacterial toxin–antitoxin systems
Published Online: Sep 17 2018
DOI: 10.1002/wrna.1506
Bacterial toxin–antitoxin systems use various mechanisms to inhibit translation and arrest growth by targeting tRNAs.
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Environmental influences on RNA processing: Biochemical, molecular and genetic regulators of cellular response
Published Online: Sep 14 2018
DOI: 10.1002/wrna.1503
The magnitude of alternative RNA processing varies across environmental contexts or cellular conditions, with different regulatory modes underlying the severity of changes.
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A recap of RNA recapping
Published Online: Sep 05 2018
DOI: 10.1002/wrna.1504
Cytoplasmic recapping is catalyzed by a complex of enzymes that restore the m7G cap onto decapped or endonucleolytically cleaved mRNAs. Recapping maintains the translation of some mRNAs and has impacts on transcriptome and proteome complexity.
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Focus Article

Dynamic and reversible RNA N 6 ‐methyladenosine methylation
Published Online: Sep 25 2018
DOI: 10.1002/wrna.1507
On messenger RNA, the reversible N6‐methyladenosine (m6A) modification is written by a m6A writer complex and erased by m6A demethylases
Abstract Full article on Wiley Online Library:   HTML | PDF

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