Biochemistry

Dock-and-lock binding of SxIP ligands is required for stable and selective EB1 interactions

1. Teresa Almeida
2. Eleanor Hargreaves
3. Tobias Zech
4. Igor Barsukov

• Curated by eLife

  eLife Assessment

  This study provides important insights into how the EBH domain of microtubule end-binding protein 1 (EB1) interacts with SxIP peptides derived from the MACF plus-end tracking protein. The revised manuscript includes convincing ITC and NMR experiments that clarify the role of flanking residues and address the influence of dimerization and cooperativity on binding. While some mechanistic aspects remain difficult to resolve experimentally, the data and analysis now more clearly justify the proposed "dock-and-lock" model and its interpretive value. This work will be of interest to structural biologists and biophysicists studying microtubule-associated protein interactions.

Reviewed by eLife

MCAK recognizes the nucleotide-dependent feature at growing microtubule ends

1. Wei Chen
2. Yin-Long Song
3. Jian-Feng He
4. Xin Liang

• Curated by eLife

  eLife Assessment

  This work presents valuable new information on the microtubule-binding mode of the microtubule kinesin-13, MCAK, the authors use quantitative single-molecule studies to propose that MCAK preferentially binds to a GDP-Pi-tubulin portion of the microtubule end. However, the evidence provided to support this claim remains incomplete and would benefit from more rigorous methodology particularly the diffraction limited experiments do not provide sufficient spatial resolution to support the authors' conclusions. In addition, a more through discussion of the existing literature would further strengthen the manuscript.

Reviewed by eLife

Chronobot: Deep learning guided time-resolved cryo-EM captures molecular choreography of RecA in homology search

1. Märt-Erik Mäeots
2. Simon Tupin
3. Mohammad M. N. Esfahani
4. Juan B. Rodriguez Molina
5. Julie A. Clapperton
6. Aran Amin
7. Albane Imbert
8. Radoslav I. Enchev

Reviewed by PREreview

Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution

1. Adrián Merino-Salomón
2. Jonathan Schneider
3. Leon Babl
4. Jan-Hagen Krohn
5. Marta Sobrinos-Sanguino
6. Tillman Schäfer
7. Juan Ramon Luque-Ortega
8. Carlos Alfonso
9. Mercedes Jiménez
10. Marion Jasnin
11. Petra Schwille
12. Germán Rivas

• Curated by eLife

  eLife Assessment

  The formation of the Z-ring at the time of bacterial cell division interests researchers working towards understanding cell division across all domains of life. The manuscript by Jasnin et al reports the cryoET structure of toroid assembly formation of FtsZ filaments driven by ZapD as the cross linker. The findings are important and have the potential to open a new dimension in the field, and the evidence to support these exciting claims is solid.

Reviewed by eLife

A miniaturized, high-throughput aqueous solvent-centric method for protein solubility screening

1. Adrian Svoboda
2. Marina Molineris
3. Theodora Tureckiova
4. Klára Hlouchová
5. Tomáš Pluskal
6. Teo Hebra

Reviewed by Arcadia Science