Biochemistry

Witnessing the structural evolution of an RNA enzyme

1. Xavier Portillo
2. Yu-Ting Huang
3. Ronald R Breaker
4. David P Horning
5. Gerald F Joyce

• Curated by eLife

  Evaluation Summary:

  The plasticity of RNA folds and their ability to response to changes in selective pressure is a key aspect of understanding the evolution of life on this planet. The Class I ligase is a remarkably fast RNA ligase ribozyme that has been harnessed by a number of laboratories to power RNA polymerization. Thought by many to be the immutable catalytic core required for polymerization, Portillo et al. demonstrate evolutionary trajectories that result in a new and catalytically enhanced ligase core. An accumulation of mutations results in a the formation of a new pseudoknot structure immediately outside the active site of the ligase core. This new structure appears to more optimally position the P7-P6-P3 coaxially stacked stems of the ligase core with respect to the primer template substrate. Tracking the emergence of this new fold, which is correlated with an enhancement in RNA polymerization activity, is novel and interesting.

  (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 #3 agreed to share their names with the authors.)

Reviewed by eLife

Visualizing formation of the active site in the mitochondrial ribosome

1. Viswanathan Chandrasekaran
2. Nirupa Desai
3. Nicholas O Burton
4. Hanting Yang
5. Jon Price
6. Eric A Miska
7. V Ramakrishnan

• Curated by eLife

  Evaluation Summary:

  Ribosomes are among the most complex molecular machines a cell makes. The work by Chandrasekaran et al. contributes to our understanding of the molecular details of mitochondrial ribosome assembly, and how disruptions to this pathway may cause human disease. Using cryo-EM, the authors identified a subpopulation of immature human mitochondrial large ribosomal subunits that interact with assembly factors NSUN4, MTERF4 and GTPBP7. Based on this structure, they introduce mutations in C. elegans orthologs of these assembly factors that are expected to disrupt binding to the large subunit, and they show that these mutants cause sterility and disrupt mitochondrial proteostasis in the mutant animals. The work does not yet establish a direct link between the putative structural defects of the mutants and the observed developmental defects in C. elegans. Additional studies are needed to test the interesting possibility that this structure represents an on-pathway intermediate of mitoribosome biogenesis and/or ribosome recycling.

  (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

Structures of SARS-CoV-2 B.1.351 neutralizing antibodies provide insights into cocktail design against concerning variants

1. Shuo Du
2. Pulan Liu
3. Zhiying Zhang
4. Tianhe Xiao
5. Ayijiang Yasimayi
6. Weijin Huang
7. Youchun Wang
8. Yunlong Cao
9. Xiaoliang Sunney Xie
10. Junyu Xiao

Reviewed by ScreenIT

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry

1. Dongxia Wang
2. Bin Zhou
3. Theodore R. Keppel
4. Maria Solano
5. Jakub Baudys
6. Jason Goldstein
7. M. G. Finn
8. Xiaoyu Fan
9. Asheley P. Chapman
10. Jonathan L. Bundy
11. Adrian R. Woolfitt
12. Sarah H. Osman
13. James L. Pirkle
14. David E. Wentworth
15. John R. Barr

Reviewed by ScreenIT

Mutations in two SARS-CoV-2 variants of concern reflect two distinct strategies of antibody escape

1. Sebastian Fiedler
2. Viola Denninger
3. Alexey S. Morgunov
4. Alison Ilsley
5. Roland Worth
6. Georg Meisl
7. Catherine K. Xu
8. Monika A. Piziorska
9. Francesco Ricci
10. Anisa Y. Malik
11. Sean R. A. Devenish
12. Matthias M. Schneider
13. Vasilis Kosmoliaptsis
14. Adriano Aguzzi
15. Akiko Iwasaki
16. Heike Fiegler
17. Tuomas P. J. Knowles

Reviewed by ScreenIT

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