Molecular Biology

N6-Adenosine Methylation of a Single Site in SARS-CoV-2 5′-UTR Promotes Translation

1. Ammar Aly
2. Gary Scott
3. Mario Calderon
4. A Pejmun Haghighi

• Curated by eLife

  eLife Assessment

  This valuable study provides solid evidence that N6 methylation of A74 by METTL3 is required for efficient translation directed by the SARS-CoV-2 5′UTR in uninfected cells, likely by limiting access of protein factors to the 5′UTR that are necessary for efficient translation. These findings advance our understanding of the role of RNA modification in coronavirus replication and m6A-mediated regulation of gene expression more broadly, while further supporting METTL3 as a potential anticoronaviral therapeutic target. However, the evidence that m6A acts by destabilizing the third stem-loop (SL3) of the 5′UTR remains incomplete. The impact of the study would be strengthened by biochemical analyses directly assessing structural changes in the 5′UTR induced by A74 methylation.

Reviewed by eLife

Site-Specific Inhibition of Translation Initiation via 2’-O-methylation

1. Adam Suh
2. Stephanie Mou
3. Emmely A. Patrasso
4. Hannah Serio
5. Kevin Vasquez
6. Rui Wang
7. Smriti Sangwan
8. Yang Yi
9. Daniel Arango

Reviewed by preLights

Stochastic splicing and deterministic inclusion of variable exons promote diversification of Down Syndrome Cell Adhesion Molecule expression

1. Anna Lassota
2. Thomas C. Dix
3. Deepanshu N. D. Singh
4. Matthias Soller

Reviewed by Review Commons

A systematic interactome of SET1C expands its functional landscape and identifies candidate regulatory connections

1. Pierre Luciano
2. Kihyun Park
3. Stéphane Audebert
4. Luc Camoin
5. Carlos A Niño
6. Da Kyeong Park
7. Isabella E Maudlin
8. Marion Dubarry
9. Lara Lee
10. Marlene Oeffinger
11. Jean D Beggs
12. Young Hye Kim
13. Jaehoon Kim
14. Bernhard Dichtl
15. Vincent Géli

• Curated by eLife

  eLife Assessment

  This study uses the yeast two-hybrid assay to identify proteins that may interact with yeast Set1 and other subunits of COMPASS/Set1C, the histone H3K4 methyltransferase, providing also some evidence for Set1 sumoylation and a role of SET1C methylating other factors in vitro. The results are valuable and they should contribute to understanding the functions of the conserved SET1C complex, as they suggest potential functional connections with RNA biogenesis, chromatin remodeling, and non-histone methylation whose implications would yet need to be explored. Nevertheless, apart from the fact that only a small subset of the Y2H interactions is further examined, the validating experiments are only partial or inconclusive, the strength of evidence being incomplete at this point, although with improvements over the previous version.

Reviewed by eLife