Biochemistry

Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation

1. Piotr Kolata
2. Rouslan G Efremov

• Curated by eLife

  Evaluation Summary:

  The manuscript reports the cryoEM structure of a functional E. coli respiratory complex I (proton-pumping NADH-ubiquinone oxidoreductase) reconstituted in lipid nano-discs. The reconstructions and models presented by the authors indicate interesting E. coli specific features of the complex, although there are some concerns about model accuracy. Overall this can be a major advance for the structure of this important respiratory complex from a key model organism.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 and Reviewer #2 agreed to share their names with the authors.)

Reviewed by eLife

Distinct shifts in site-specific glycosylation pattern of SARS-CoV-2 spike proteins associated with arising mutations in the D614G and Alpha variants

1. Chu-Wei Kuo
2. Tzu-Jing Yang
3. Yu-Chun Chien
4. Pei-Yu Yu
5. Shang-Te Danny Hsu
6. Kay-Hooi Khoo

Reviewed by ScreenIT

PDZ-Containing Proteins Targeted by the ACE2 Receptor

1. Célia Caillet-Saguy
2. Nicolas Wolff

Reviewed by ScreenIT

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain

1. Edgar E Boczek
2. Julius Fürsch
3. Marie Laura Niedermeier
4. Louise Jawerth
5. Marcus Jahnel
6. Martine Ruer-Gruß
7. Kai-Michael Kammer
8. Peter Heid
9. Laura Mediani
10. Jie Wang
11. Xiao Yan
12. Andrej Pozniakovski
13. Ina Poser
14. Daniel Mateju
15. Lars Hubatsch
16. Serena Carra
17. Simon Alberti
18. Anthony A Hyman
19. Florian Stengel

• Curated by eLife

  Evaluation Summary:

  This work traces at the protein domain level the associations made within droplets containing RNA-binding protein FUS and how they change as a function of time (and maturity), in the presence and absence of the small heat-shock protein HSPB8, by chemical cross-linking coupled to mass spectrometry. This work is an important step forward in our general understanding of the macromolecular interactions within liquid-liquid phase-separated protein droplets, and how they are regulated by small heat-shock protein molecular chaperones.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1, #2, and #3 agreed to shares their name with the authors.)

Reviewed by eLife

A Highly Potent SARS-CoV-2 Blocking Lectin Protein

1. Recep E. Ahan
2. Alireza Hanifehnezhad
3. Ebru Ş. Kehribar
4. Tuba C. Oguzoglu
5. Katalin Földes
6. Cemile E. Özçelik
7. Nazlican Filazi
8. Sıdıka Öztop
9. Fahreddin Palaz
10. Sevgen Önder
11. Eray U. Bozkurt
12. Koray Ergünay
13. Aykut Özkul
14. Urartu Özgür Şafak Şeker

Reviewed by ScreenIT

Discovery of nanobodies against SARS-CoV-2 and an uncommon neutralizing mechanism

1. Tingting Li
2. Bingjie Zhou
3. Zhipu Luo
4. Yanling Lai
5. Suqiong Huang
6. Yuanze Zhou
7. Anupriya Gautam
8. Salome Bourgeau
9. Shurui Wang
10. Juan Bao
11. Jingquan Tan
12. Dimitri Lavillette
13. Dianfan Li

Reviewed by ScreenIT

Edge-strand of BepA interacts with immature LptD on the β-barrel assembly machine to direct it to on- and off-pathways

1. Ryoji Miyazaki
2. Tetsuro Watanabe
3. Kohei Yoshitani
4. Yoshinori Akiyama

• Curated by eLife

  Evaluation Summary:

  This study reports a pivotal role of the conserved edge-strand of the periplasmic metalloprotease BepA in the folding and quality control of an outer membrane protein (OMP), the lipopolysaccharide transporter LptD, in gram-negative bacteria. The authors have discovered that, in addition to proteolytic activity, BepA has a chaperone-like activity and that BepA-mediated quality control of LptD and likely other OMPs occurs during their membrane insertion at the barrel assembly machinery. This result provides new insights into the biogenesis mechanisms of bacterial OMPs and the maintenance of OM integrity.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 and Reviewer #2 agreed to share their names with the authors.)

Reviewed by eLife

GFPT2/GFAT2 and AMDHD2 act in tandem to control the hexosamine pathway

1. Virginia Kroef
2. Sabine Ruegenberg
3. Moritz Horn
4. Kira Allmeroth
5. Lena Ebert
6. Seyma Bozkus
7. Stephan Miethe
8. Ulrich Elling
9. Bernhard Schermer
10. Ulrich Baumann
11. Martin Sebastian Denzel

• Curated by eLife

  Evaluation Summary:

  This manuscript describes an interesting regulation of the hexosamine biosynthetic pathway (HBP) that is relative specific to the mouse embryonic stem cells (mESC). HBP produces UDP-N-acetylglucosamine, which is used in various protein glycosylation events, thus regulating many biological pathways. Understanding this pathway and its regulation is thus of fundamental significance.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 agreed to share their name with the authors.)

Reviewed by eLife

Principles of RNA recruitment to viral ribonucleoprotein condensates in a segmented dsRNA virus

1. Sebastian Strauss
2. Julia Acker
3. Guido Papa
4. Daniel Desirò
5. Florian Schueder
6. Alexander Borodavka
7. Ralf Jungmann

• Curated by eLife

  Evaluation Summary:

  This study will be of interest to virologists and those working on RNA-protein particles. Strauss and colleagues studied the mechanism of RNA recruitment to ribonucleoprotein condensates using rotavirus. Using multiplexed DNA-barcorded smFISH and DNA-PAINT for direct visualization of the RNP condensates in cells, they observe the early onset of viral transcript oligomerization before the formation of viroplasms and the process of enrichment in RNP condensates. They were able to image all eleven transcripts in an RNP condensate and to quantify the amounts of these transcripts. Based on these findings, the authors suggest a selective RNA enrichment mechanism of rotavirus. The experiments are nicely executed, with good controls.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 agreed to share their name with the authors.)

Reviewed by eLife

Increased histone-DNA complexes and endothelial-dependent thrombin generation in severe COVID-19

1. Beth A. Bouchard
2. Christos Colovos
3. Michael A. Lawson
4. Zachary T. Osborn
5. Adrian M. Sackheim
6. Kara J. Mould
7. William J. Janssen
8. Mitchell J. Cohen
9. Devdoot Majumdar
10. Kalev Freeman

Reviewed by ScreenIT