Biochemistry

A methylation-phosphorylation switch controls EZH2 stability and hematopoiesis

1. Pengfei Guo
2. Rebecca C Lim
3. Keshari Rajawasam
4. Tiffany Trinh
5. Hong Sun
6. Hui Zhang

• Curated by eLife

  eLife assessment

  This is a fundamental study describing a novel methylation event on EZH2 that regulates EZH2 protein stability and hematopoiesis. The methodologies are sound and the conclusions are largely supported by solid data. The work will be of interest to biomedical researchers in the field of cancer epigenetics.

Reviewed by eLife

Noncanonical usage of stop codons in ciliates expands proteins with structurally flexible Q-rich motifs

1. Chi-Ning Chuang
2. Hou-Cheng Liu
3. Tai-Ting Woo
4. Ju-Lan Chao
5. Chiung-Ya Chen
6. Hisao-Tang Hu
7. Yi-Ping Hsueh
8. Ting-Fang Wang

• Curated by eLife

  eLife assessment

  This study presents useful results on glutamine-rich motifs in relation to protein expression and alternative genetic codes. The solid data are based on bioinformatic approaches that are employed to systematically uncover sequence features associated with proteome-wide amino acid distribution and biological processes.

Reviewed by eLife

An engineered biosensor enables dynamic aspartate measurements in living cells

1. Kristian Davidsen
2. Jonathan S Marvin
3. Abhi Aggarwal
4. Timothy A Brown
5. Lucas B Sullivan

• Curated by eLife

  eLife assessment

  This important study reports jAspSnFR3, a biosensor that enables high spatiotemporal resolution of aspartate levels in living cells. To develop this sensor, the authors used a structurally guided amino acid substitution in a glutamate/aspartate periplasmic binding protein to switch its specificity towards aspartate. The in vitro and in cellulo functional characterization of the biosensor is convincing, but evidence of the sensor's effectiveness in detecting small perturbations of aspartate levels and information on its behavior in response to acute aspartate elevations in the cytosol are still lacking.

Reviewed by eLife

Structural and biophysical analysis of a Haemophilus influenzae tripartite ATP-independent periplasmic (TRAP) transporter

1. Michael J Currie
2. James S Davies
3. Mariafrancesca Scalise
4. Ashutosh Gulati
5. Joshua D Wright
6. Michael C Newton-Vesty
7. Gayan S Abeysekera
8. Ramaswamy Subramanian
9. Weixiao Y Wahlgren
10. Rosmarie Friemann
11. Jane R Allison
12. Peter D Mace
13. Michael DW Griffin
14. Borries Demeler
15. Soichi Wakatsuki
16. David Drew
17. Cesare Indiveri
18. Renwick CJ Dobson
19. Rachel A North

• Curated by eLife

  eLife assessment

  The current manuscript presents a cryo-EM structure of a tripartite ATP-independent periplasmic (TRAP) transporter that contributes to Haemophilus influenzae virulence. Convincing biophysical and cryo-EM experiments yield a valuable molecular model, but the functional importance of some of the molecular features identified remains to be demonstrated.

Reviewed by eLife

Structure and function of bacterial YeeE-YeeD complex in thiosulfate uptake pathway

1. Mai Ikei
2. Ryoji Miyazaki
3. Keigo Monden
4. Yusuke Naito
5. Azusa Takeuchi
6. Yutaro S. Takahashi
7. Yoshiki Tanaka
8. Keina Murata
9. Takaharu Mori
10. Muneyoshi Ichikawa
11. Tomoya Tsukazaki

Reviewed by Review Commons

Structure of an open K _ATP channel reveals tandem PIP ₂ binding sites mediating the Kir6.2 and SUR1 regulatory interface

1. Camden M. Driggers
2. Yi-Ying Kuo
3. Phillip Zhu
4. Assmaa ElSheikh
5. Show-Ling Shyng

• Curated by Biophysics Colab

  Evaluation statement (10 January 2024)

  Driggers et al. is an elegant study that reports the structure of an open KATP channel complex formed from the Q52R diabetes mutation of the pore-forming subunit Kir 6.2, the sulfonylurea receptor (SUR1), and long-chain phosphatidylinositol 4,5-bisphosphate (PIP2) – a key lipid that stabilizes the open state of the channel and regulates inhibition by intracellular ATP. The structure reveals one PIP2 site related to that seen in other Kir channels as well as a second unanticipated one where the lipid snuggles into the interface between Kir6.2 and a region of SUR1 previously implicated in promoting the open state of KATP. This important finding helps to explain how PIP2 exerts such a profound regulatory influence on KATP.

  Biophysics Colab considers this to be a convincing study and recommends it to scientists working on KATP and other membrane proteins regulated by PIP2.

  (This evaluation by Biophysics Colab refers to version 2 of this preprint, which has been revised in response to peer review of version 1.)

Reviewed by Biophysics Colab

Molecular dissection of PI3Kβ synergistic activation by receptor tyrosine kinases, GβGγ, and Rho-family GTPases

1. Benjamin R Duewell
2. Naomi E Wilson
3. Gabriela M Bailey
4. Sarah E Peabody
5. Scott D Hansen

• Curated by eLife

  eLife assessment

  The manuscript describes the synergy among PI3Kbeta activators, providing compelling results concerning the mechanism of their activation. The particular strengths of the work arise to a great extend from the reconstitution system better mimicking the natural environment of the plasma membrane than previous setups have. The study will be a landmark contribution to the signaling field.

Reviewed by eLife

Novel sterol binding domains in bacteria

1. Liting Zhai
2. Amber C Bonds
3. Clyde A Smith
4. Hannah Oo
5. Jonathan Chiu-Chun Chou
6. Paula V Welander
7. Laura MK Dassama

• Curated by eLife

  eLife assessment

  This is a valuable contribution to our understanding of how some bacteria can transport sterols from the cytoplasm to the outer membrane. Though much remains to be tested and explored, the data and analyses presented here provide solid evidence for the genetic and physical interaction of BstA/B/C with bacterially-produced sterols. The manuscript will be of interest to scientists focusing on the characterization of novel bacterial proteins and those studying lipid transport and acquisition in bacterial pathogens.

Reviewed by eLife

Disordered regions and folded modules in CAF-1 promote histone deposition in Schizosaccharomyces pombe

1. Fouad Ouasti
2. Maxime Audin
3. Karine Fréon
4. Jean-Pierre Quivy
5. Mehdi Tachekort
6. Elizabeth Cesard
7. Aurélien Thureau
8. Virginie Ropars
9. Paloma Fernández Varela
10. Gwenaelle Moal
11. Ibrahim Soumana-Amadou
12. Aleksandra Uryga
13. Pierre Legrand
14. Jessica Andreani
15. Raphaël Guerois
16. Geneviève Almouzni
17. Sarah Lambert
18. Francoise Ochsenbein

• Curated by eLife

  eLife assessment

  This important study advances our understanding of the machinery that couples DNA synthesis with the deposition of histone proteins onto newly synthesized DNA. A convincing array of experiments combines NMR, protein biochemistry, and in vivo analyses of Chromatin Assembly Factor-1 of fission yeast. The work is of interest to researchers in the field of chromosome/chromatin biology as well as epigenetics.

Reviewed by eLife

Acyl-CoA thioesterase-2 facilitates β-oxidation in glycolytic skeletal muscle in a lipid supply dependent manner

1. Carmen Bekeova
2. Ji In Han
3. Heli Xu
4. Evan Kerr
5. Brittney Blackburne
6. Shannon C. Lynch
7. Clementina Mesaros
8. Marta Murgia
9. Rajanikanth Vadigepalli
10. Joris Beld
11. Roberta Leonardi
12. Nathaniel W. Snyder
13. Erin L. Seifert

• Curated by eLife

  eLife assessment

  This study presents new data highlighting the importance of appropriate coenzyme A handling in the mitochondria for maintaining appropriate energy production capacity. Several findings regarding the role of a key metabolic enzyme in how skeletal muscle cells use different substrates for energy production are valuable and supported by solid evidence, but there are concerns whether the data support the conclusion that ACOT2 regulates mitochondrial matrix acyl-CoA levels in white skeletal muscle to facilitate fatty acid oxidation β-oxidation.

Reviewed by eLife