Biochemistry

Semi‐synthetic nanobody‐ligand conjugates exhibit tunable signaling properties and enhanced transcriptional outputs at neurokinin receptor‐1

1. Nayara Braga Emidio
2. Ross W. Cheloha

Reviewed by Biophysics Colab

Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation

1. Raphael Trenker
2. Devan Diwanji
3. Tanner Bingham
4. Kliment A Verba
5. Natalia Jura

• Curated by eLife

  eLife assessment

  This manuscript describes structures of HER4 homo- and HER4/HER2 hetero-dimer complexes using single particle cryo-EM. This important work describes convincingly new structural details of these complexes that expand our understanding of their function. This work will be of interest to researchers working on cell surface signalling and kinase activity.

Reviewed by eLife

Guanidine production by plant homoarginine-6-hydroxylases

1. Dietmar Funck
2. Malte Sinn
3. Giuseppe Forlani
4. Jörg S Hartig

• Curated by eLife

  eLife assessment

  This fundamental study advances our understanding of nitrogen metabolism by identifying a new type of guanidine-forming enzyme in eukaryotes. The key claims of the article are convincingly supported by the data, with meticulous biochemical, cellular, and in vivo studies on guanidine production. The work will stimulate interest in the cellular roles of homoarginine, and, more generally, in the biochemistry and metabolism of guanidine derivatives.

Reviewed by eLife

Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock

1. Daniyal Tariq
2. Nicole Maurici
3. Bradley M Bartholomai
4. Siddarth Chandrasekaran
5. Jay C Dunlap
6. Alaji Bah
7. Brian R Crane

• Curated by eLife

  eLife assessment

  This manuscript is a fundamental contribution to the understanding of the role of intrinsically disordered proteins in circadian clocks and the potential involvement of phase separation mechanisms. The authors convincingly report on the structural and biochemical aspects and the molecular interactions of the intrinsically disordered protein FRQ. The paper will be of interest to scientists focusing on circadian clock regulation, liquid-liquid phase separation, and phosphorylation.

Reviewed by eLife

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

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