Biochemistry

Caenorhabditis elegans Dicer acts with the RIG-I-like helicase DRH-1 and RDE-4 to cleave dsRNA

1. Claudia D Consalvo
2. Adedeji M Aderounmu
3. Helen M Donelick
4. P Joseph Aruscavage
5. Debra M Eckert
6. Peter S Shen
7. Brenda L Bass

• Curated by eLife

  eLife assessment

  To investigate the evolutionary relationship between the RNAi pathway and innate immunity, this valuable study uses biochemistry and structural biology to investigate the trimeric complex of Dicer-1, DRH-1 (a RIGI homologue), and RDE-4, which exists in C. elegans. The results described include rigorous kinetic analysis of the enzymatic activity of the complex and a moderate resolution cryo-EM structure. The results are convincing and add to the broader understanding of the evolution of antiviral defense.

Reviewed by eLife

Giardia intestinalis deoxyadenosine kinase has a unique tetrameric structure that enables high substrate affinity and makes the parasite sensitive to deoxyadenosine analogues

1. Farahnaz Ranjbarian
2. Karim Rafie
3. Kasturika Shankar
4. Sascha Krakovka
5. Staffan G. Svärd
6. Lars-Anders Carlson
7. Anders Hofer

Reviewed by Review Commons

CK-666 and CK-869 differentially inhibit Arp2/3 iso-complexes

1. LuYan Cao
2. Shaina Huang
3. Angika Basant
4. Miroslav Mladenov
5. Michael Way

Reviewed by Review Commons

Transcriptome-wide analysis of the function of Ded1 in translation preinitiation complex assembly in a reconstituted in vitro system

1. Fujun Zhou
2. Julie M Bocetti
3. Meizhen Hou
4. Daoming Qin
5. Alan G Hinnebusch
6. Jon R Lorsch

• Curated by eLife

  eLife assessment

  This is an important paper as it is the first to use a reconstituted translation system to study competition among mRNAs for the initiation machinery. Understanding the principles of the biochemistry of mRNA competition for initiation factors cannot be achieved without such a system. The authors provide compelling evidence that Ded1 is required for efficient initiation of highly structured mRNAs. The findings are significant and validate the in vitro reconstituted system by recapitulating the effects of in-vivo perturbations of translation initiation by Ded1 mutants.

Reviewed by eLife

Viral proteins activate PARIS-mediated tRNA degradation and viral tRNAs rescue infection

1. Nathaniel Burman
2. Svetlana Belukhina
3. Florence Depardieu
4. Royce A. Wilkinson
5. Mikhail Skutel
6. Andrew Santiago-Frangos
7. Ava B. Graham
8. Alexei Livenskyi
9. Anna Chechenina
10. Natalia Morozova
11. Trevor Zahl
12. William S. Henriques
13. Murat Buyukyoruk
14. Christophe Rouillon
15. Lena Shyrokova
16. Tatsuaki Kurata
17. Vasili Hauryliuk
18. Konstantin Severinov
19. Justine Groseille
20. Agnès Thierry
21. Romain Koszul
22. Florian Tesson
23. Aude Bernheim
24. David Bikard
25. Blake Wiedenheft
26. Artem Isaev

Reviewed by Rapid Reviews Infectious Diseases

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin

1. Ao Liu
2. Anna L. Hatch
3. Henry N. Higgs

Reviewed by Review Commons

Fascin-induced bundling protects actin filaments from disassembly by cofilin

1. Jahnavi Chikireddy
2. Léana Lengagne
3. Rémi Le Borgne
4. Catherine Durieu
5. Hugo Wioland
6. Guillaume Romet-Lemonne
7. Antoine Jégou

Reviewed by Review Commons

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase

1. Valentin Bohl
2. Nele Merret Hollmann
3. Tobias Melzer
4. Panagiotis Katikaridis
5. Lena Meins
6. Bernd Simon
7. Dirk Flemming
8. Irmgard Sinning
9. Janosch Hennig
10. Axel Mogk

• Curated by eLife

  eLife assessment

  This important manuscript details the characterization of ClpL from L. monocytogenes as an effective and autonomous AAA+ disaggregase that provides enhanced heat resistance to this food-borne pathogen. Supported by compelling evidence, the authors demonstrate that ClpL has DnaK-independent disaggregase activity towards a variety of aggregated model substrates, which is more potent than that observed with the endogenous canonical DnaK/ClpB bi-chaperone system. The work will be of broad interest to microbiologists and biochemists.

Reviewed by eLife

X-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX

1. Isabelle Petit-Hartlein
2. Annelise Vermot
3. Michel Thepaut
4. Anne-Sophie Humm
5. Florine Dupeux
6. Jerome Dupuy
7. Vincent Chaptal
8. Jose Antonio Marquez
9. Susan ME Smith
10. Franck Fieschi

• Curated by eLife

  eLife assessment

  In this manuscript, the authors investigate the properties of prokaryotic NADPH oxidases (NOX) and discuss the implications for NOX regulation and function. The structure of the S. pneumoniae Nox protein is an important step forward in our understanding of procaryotic NOX enzymes and the characterization and interpretation are convincing. The results will be of interest to structural biologists as well as biochemists focusing on enzymatic functions.

Reviewed by eLife

The C-terminus of CFAP410 forms a tetrameric helical bundle that is essential for its localization to the basal body

1. Alexander Stadler
2. Laryssa V. De Liz
3. Heloisa B. Gabriel
4. Santiago Alonso-Gil
5. Robbie Crickley
6. Katharina Korbula
7. Bojan Žagrović
8. Sue Vaughan
9. Jack D. Sunter
10. Gang Dong

Reviewed by Review Commons