Biochemistry

Mag-Net: Rapid enrichment of membrane-bound particles enables high coverage quantitative analysis of the plasma proteome

1. Christine C. Wu
2. Kristine A. Tsantilas
3. Jea Park
4. Deanna Plubell
5. Justin A. Sanders
6. Previn Naicker
7. Ireshyn Govender
8. Sindisiwe Buthelezi
9. Stoyan Stoychev
10. Justin Jordaan
11. Gennifer Merrihew
12. Eric Huang
13. Edward D. Parker
14. Michael Riffle
15. Andrew N. Hoofnagle
16. William S. Noble
17. Kathleen L. Poston
18. Thomas J. Montine
19. Michael J. MacCoss

Reviewed by PREreview

A unique cell division protein critical for the assembly of the bacterial divisome

1. Xiao Chu
2. Lidong Wang
3. Yiheng Zhu
4. Zhengshan Feng
5. Qingtian Guan
6. Lei Song
7. Zhaoqing Luo

• Curated by eLife

  eLife assessment:

  This useful study shows that the essential Acinetobacter baumannii gene Aeg1 likely plays an key role in cell division. The strength of the work is the discovery that the depletion of Aeg1 leads to cell filamentation and that gain-of-function mutations in cell division genes FtsB and FtsL rescue the lethality of Aeg1 depletion. However, Aeg1's localization pattern and its requirement for other division proteins' localizations require further characterization of the functionality of fluorescent fusion proteins, fluorescence images of higher quality, and improvements in statistic qualifications, leaving the study' evidence for Aeg1's exact role in cell division incomplete at this time. In conclusion, the critical role of Aeg1 in the assembly of the A. baumannii divisome has yet to be established unambiguously.

Reviewed by eLife, Arcadia Science

Activation of polycystin-1 signaling by binding of stalk-derived peptide agonists

1. Shristi Pawnikar
2. Brenda S Magenheimer
3. Keya Joshi
4. Ericka Nevarez-Munoz
5. Allan Haldane
6. Robin L Maser
7. Yinglong Miao

• Curated by eLife

  eLife assessment

  This joint computational/experimental study demonstrates the ability of synthetic peptides derived from the stalk-tethered agonist in Polycystin-1 (PC1) to re-activate signaling by a stalkless C-terminal fragment of PC1. The study is valuable as it discovered peptide agonists for PC1 and the integrated in vitro and in silico approach is potentially applicable to the analysis of related systems. Following the revision, the line of evidence presented in the current manuscript is considered convincing.

Reviewed by eLife

Structure and evolution of alanine/serine decarboxylases and the engineering of theanine production

1. Hao Wang
2. Biying Zhu
3. Siming Qiao
4. Chunxia Dong
5. Xiaochun Wan
6. Weimin Gong
7. Zhaoliang Zhang

• Curated by eLife

  eLife assessment

  This study reports a comparative biochemical and structural analysis of two PLP decarboxylase enzymes from plants. The work is useful because of the potential application of these enzymes in industrial theanine production. The structure provides a solid basis for understanding substrate specificity but some aspects of the work are incomplete. The paper will be of interest to enzymologists studying PLP enzymes and those working on enzyme engineering in plants.

Reviewed by eLife

Cyanobacteria form a procarboxysome-like structure in response to high CO ₂

1. Clair A. Huffine
2. Catherine Fontana
3. Anton Avramov
4. Colin Sempeck
5. Jeffrey C. Cameron

Reviewed by PREreview

Observing one-divalent-metal-ion-dependent and histidine-promoted His-Me family I-PpoI nuclease catalysis in crystallo

1. Caleb Chang
2. Grace Zhou
3. Yang Gao

• Curated by eLife

  eLife assessment

  Chang et al. have investigated the catalytic mechanism of I-PpoI nuclease, a one-metal-ion dependent nuclease, by time-resolved X-ray crystallography using soaking of crystals with metal ions under different pH conditions. This convincing study revealed that I-PpoI catalyzes the reaction process through a single divalent cation. The study uncovers important details of the roles of the metal ion and the active site histidine in catalysis.

Reviewed by eLife

A substrate-interacting region of Parkin directs ubiquitination of the mitochondrial GTPase Miro1

1. Joanna Koszela
2. Anne Rintala-Dempsey
3. Giulia Salzano
4. Viveka Pimenta
5. Outi Kamarainen
6. Mads Gabrielsen
7. Aasna L. Parui
8. Gary S. Shaw
9. Helen Walden

Reviewed by Review Commons

Cryo-EM structure of the bicarbonate receptor GPR30

1. Shota Kaneda
2. Airi Jo-Watanabe
3. Hiroaki Akasaka
4. Hidetaka S Oshima
5. Takehiko Yokomizo
6. Wataru Shihoya
7. Osamu Nureki

• Curated by eLife

  eLife assessment

  This study resolves a cryo-EM structure of the GPCR, human GPR30, which responds to bicarbonate and regulates cellular responses to pH and ion homeostasis. Understanding the ligand and the mechanism of activation is important to the field of receptor signaling and potentially facilitates drug development targeting this receptor. While the overall structures are solid, the identification of the bicarbonate binding site is only partly supported by the structural data and cell-based functional assays, leaving a major aim of the study incomplete.

Reviewed by eLife

Tryptanthrin Analogs Substoichiometrically Inhibit Seeded and Unseeded Tau4RD Aggregation

1. Ellie I James
2. David W Baggett
3. Edcon Chang
4. Joel Schachter
5. Thomas Nixey
6. Karoline Choi
7. Miklos Guttman
8. Abhinav Nath

• Curated by eLife

  eLife assessment

  This study provides a valuable contribution to the development of small molecules that inhibit the aggregation of tau, a protein involved in several neurodegenerative diseases. The authors present convincing evidence that analogs of the plant alkaloid tryptanthrin can prevent the formation of larger aggregates by targeting the early stages of tau oligomerization. Nevertheless, further studies are needed to elucidate the precise mechanisms of action and to provide a detailed kinetic analysis. This work will be of interest to biochemists and biophysicists focused on designing small molecules to inhibit fibril formation.

Reviewed by eLife

Effects of Gallic Acid on Antioxidant Defense System in Mice with Benzene-Induced Myelotoxicity

1. Toba Isaac Olatoye
2. Joseph O. Adebayo

Reviewed by PREreview