Biochemistry

YeeD is an essential partner for YeeE-mediated thiosulfate uptake in bacteria and regulates thiosulfate ion decomposition

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 KATP channel reveals tandem PIP2 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 Adamou
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

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions

1. Jixing Lyu
2. Tianqi Zhang
3. Michael T Marty
4. David Clemmer
5. David H Russell
6. Arthur Laganowsky

• Curated by eLife

  eLife assessment

  This is an important biophysical study combining native mass spectrometry with mutant cycles to estimate the thermodynamic components of lipid A binding to the ABC transporter MsbA. Solid evidence supports the binding energies for lipid-protein interactions to MsbA using this approach, which could be later applied to other membrane proteins in general.

Reviewed by eLife

The role of RNA in the maintenance of chromatin domains as revealed by antibody-mediated proximity labelling coupled to mass spectrometry

1. Rupam Choudhury
2. Anuroop Venkateswaran Venkatasubramani
3. Jie Hua
4. Marco Borsò
5. Celeste Franconi
6. Sarah Kinkley
7. Ignasi Forné
8. Axel Imhof

Reviewed by Review Commons

Conformation selection by ATP-competitive inhibitors and allosteric communication in ERK2

1. Jake W Anderson
2. David Vaisar
3. David N Jones
4. Laurel M Pegram
5. Guy P Vigers
6. Huifen Chen
7. John G Moffat
8. Natalie G Ahn

• Curated by eLife

  eLife assessment

  This fundamental study provides compelling evidence to explain how chemical variations within a set of kinase inhibitors drive the selection of specific Erk2 conformations. Conformational selection plays a critical role in targeting medically relevant kinases such as Erk2 and the findings reported here open new avenues for designing small molecule inhibitors that block the active site while also steering the population of the enzyme into active or inactive conformations. Since protein dynamics and conformational ensembles are essential for enzyme function, this work will be of broad interest to those working in drug development, signal transduction, and enzymology.

Reviewed by eLife

Dual recognition of multiple signals in bacterial outer membrane proteins enhances assembly and maintains membrane integrity

1. Edward M Germany
2. Nakajohn Thewasano
3. Kenichiro Imai
4. Yuki Maruno
5. Rebecca S Bamert
6. Christopher J Stubenrauch
7. Rhys A Dunstan
8. Yue Ding
9. Yukari Nakajima
10. XiangFeng Lai
11. Chaille T Webb
12. Kentaro Hidaka
13. Kher Shing Tan
14. Hsinhui Shen
15. Trevor Lithgow
16. Takuya Shiota

• Curated by eLife

  eLife assessment

  This important study reports the identification of a new amino acid sequence motif (i.e., "internal beta-signal") on outer membrane proteins, which is recognized by beta-assembly machinery in gram-negative bacteria. The authors carried out rigorous experiments, providing compelling evidence in support of their conclusions. This work significantly advances our understanding of the biogenesis of outer membrane proteins.

Reviewed by eLife