Wilson Lab's Avatar

Wilson Lab

@wilsonlab.bsky.social

Ribosomes & Translation Regulation; Antibiotics & Resistance Mechanisms; Structural Biology & Cryo-EM; University of Hamburg.

540 Followers  |  114 Following  |  33 Posts  |  Joined: 08.12.2023  |  1.8753

Latest posts by wilsonlab.bsky.social on Bluesky

Preview
Structural biologist Alexey Amunts launches new research lab in Shenzhen β€˜Shenzhen adds another dimension; it is a place where ideas do not remain ideas for long,’ Amunts says of new position.

We're launching a research lab at SMART. Shenzhen Medical Academy for Research and Translation is a newly established institute with long-term funding mechanisms for internal and external investigators. At full capacity SMART aims to support up to 400 labs.
www.scmp.com/news/china/s...

06.02.2026 05:33 β€” πŸ‘ 66    πŸ” 18    πŸ’¬ 2    πŸ“Œ 2
Preview
Yeast elongation factor homolog New1 protects a subset of mRNAs from degradation by no-go decay Abstract. New1 is a homologue of the essential yeast translation elongation factor eEF3. Lack of New1 has been shown to induce ribosome queuing upstream of

4 - Still lots to learn about this mysterious factor.
πŸ”— Read the paper: academic.oup.com/nar/article/...
Funded by @dfg.de via SFB TRR319-RMaP πŸ™
#RibosomeBiology #TranslationQC #RNA #Nanopore #Yeast #PhDPosition #DFG #RMaP #New1

01.02.2026 21:53 β€” πŸ‘ 14    πŸ” 11    πŸ’¬ 1    πŸ“Œ 0

3 - Builds on work from @hauryliuk.bsky.social & @wilsonlab.bsky.social.

Big thanks to our collaborators Liz Petfalski, Tamer Butto and Stefan Pastore, and huge kudos to main heroes from Winz lab: Max MΓΌller and Lena Tittel, as well as @kaushikiyer.bsky.social, and Alina-Andrea Kraft!

01.02.2026 21:51 β€” πŸ‘ 1    πŸ” 1    πŸ’¬ 0    πŸ“Œ 0
Bacterial defense via RES-mediated NAD+ depletion is countered by phage phosphatases Many bacterial defense systems restrict phage infection by breaking the molecule NAD+ to its constituents, adenosine diphosphate ribose (ADPR) and nicotinamide (Nam). To counter NAD+ depletion-mediated defense, phages evolved NAD+ reconstitution pathway 1 (NARP1), which uses ADPR and Nam to rebuild NAD+. Here we report a bacterial defense system called aRES, involving RES-domain proteins that degrade NAD+ into Nam and ADPR-1β€³-phosphate (ADPR-1P). This molecule cannot serve as a substrate for NARP1, so that NAD+ depletion by aRES defends against phages even if they encode NARP1. We further discover that some phages evolved an extended NARP1 pathway capable of overcoming aRES defense. In these phages, the NARP1 operon also includes a specialized phosphatase, which dephosphorylates ADPR-1P to form ADPR, a substrate from which NARP1 then reconstitutes NAD+. Other phages encode inhibitors that directly bind aRES proteins and physically block their active sites. Our study describes new layers in the NAD+-centric arms race between bacteria and phages and highlights the centrality of the NAD+ pool in cellular battles between viruses and their hosts. ### Competing Interest Statement The authors have declared no competing interest. European Research Council, ERC-AdG GA 101018520 Israel Science Foundation, MAPATS grant 2720/22 Deutsche Forschungsgemeinschaft, SPP 2330, grant 464312965 Minerva Foundation with funding from the Federal German Ministry for Education and Research research grant from Magnus Konow in honor of his mother Olga Konow Rappaport Ministry of Aliyah and Immigrant Absorption, https://ror.org/05aycsg86 Clore Scholars Program

🧬 Metabolic arms race continues!
We discovered a new NAD⁺-depleting bacterial immune system aRES and phage enzymes that overcome it.
Our preprint is out: www.biorxiv.org/content/10.6...

29.01.2026 11:20 β€” πŸ‘ 29    πŸ” 17    πŸ’¬ 1    πŸ“Œ 5

Have a look at our new structure of co translational folding in yeast. This is collaborative work initialized by the Rospert lab from the @uni-freiburg.de. Structural work has been done by the amazing @lgrundmann.bsky.social Stay tuned for the next ribosome paper from him, following very soon.

19.01.2026 11:09 β€” πŸ‘ 41    πŸ” 15    πŸ’¬ 1    πŸ“Œ 0
Bacterial defense via RES-mediated NAD+ depletion is countered by phage phosphatases Many bacterial defense systems restrict phage infection by breaking the molecule NAD+ to its constituents, adenosine diphosphate ribose (ADPR) and nicotinamide (Nam). To counter NAD+ depletion-mediated defense, phages evolved NAD+ reconstitution pathway 1 (NARP1), which uses ADPR and Nam to rebuild NAD+. Here we report a bacterial defense system called aRES, involving RES-domain proteins that degrade NAD+ into Nam and ADPR-1β€³-phosphate (ADPR-1P). This molecule cannot serve as a substrate for NARP1, so that NAD+ depletion by aRES defends against phages even if they encode NARP1. We further discover that some phages evolved an extended NARP1 pathway capable of overcoming aRES defense. In these phages, the NARP1 operon also includes a specialized phosphatase, which dephosphorylates ADPR-1P to form ADPR, a substrate from which NARP1 then reconstitutes NAD+. Other phages encode inhibitors that directly bind aRES proteins and physically block their active sites. Our study describes new layers in the NAD+-centric arms race between bacteria and phages and highlights the centrality of the NAD+ pool in cellular battles between viruses and their hosts. ### Competing Interest Statement The authors have declared no competing interest. European Research Council, ERC-AdG GA 101018520 Israel Science Foundation, MAPATS grant 2720/22 Deutsche Forschungsgemeinschaft, SPP 2330, grant 464312965 Minerva Foundation with funding from the Federal German Ministry for Education and Research research grant from Magnus Konow in honor of his mother Olga Konow Rappaport Ministry of Aliyah and Immigrant Absorption, https://ror.org/05aycsg86 Clore Scholars Program

We found a new mode by which bacteria deplete NAD+ to protect from phages. And then we found how phages overcome this defense

Discovered by talented biochemist Dr Ilya Osterman, read the preprint: tinyurl.com/Narp-ap

A thread 🧡

29.01.2026 15:34 β€” πŸ‘ 44    πŸ” 15    πŸ’¬ 2    πŸ“Œ 0
Preview
Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus Lawrence et al. examine how ribosome production in the eukaryotic nucleolus is coordinated by cytoplasmic processes to maintain appropriate ribosome numbers. The authors highlight regulatory inputs from cytoplasmic signaling, mitosis, and cytoplasmic organelles that converge on nucleolar function, and they discuss how disruption of these pathways contributes to human disease.

Online Now: Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus Online now:

28.01.2026 23:57 β€” πŸ‘ 9    πŸ” 8    πŸ’¬ 0    πŸ“Œ 0
Preview
Structures of naked mole-rat, tuco-tuco, and guinea pig ribosomesβ€”is rRNA fragmentation linked to translational fidelity? Abstract. Ribosomes are central to protein synthesis in all organisms. In mammals, the ribosome functional core is highly conserved. Remarkably, two rodent

now online:
academic.oup.com/nar/article/...

29.01.2026 13:47 β€” πŸ‘ 16    πŸ” 11    πŸ’¬ 3    πŸ“Œ 1
Preview
ADAM-tRNA-seq: an optimized approach for demultiplexing and enhanced hierarchal mapping in direct tRNA sequencing Abstract. Transfer RNAs (tRNAs) play an essential role in protein synthesis and cellular homeostasis, and their dysregulation is associated with various hu

Interested in direct tRNA-seq by Nanopore? We developed a new RNA-based barcoding aproach for seq parallelization; it is also cost-saving. Scripts available on github. #tRNA #Nanopore

track.smtpsendmail.com/9032119/c?p=...

27.01.2026 22:14 β€” πŸ‘ 24    πŸ” 9    πŸ’¬ 1    πŸ“Œ 1

Active transport of tRNAs facilitates distributed protein synthesis https://www.biorxiv.org/content/10.64898/2026.01.26.698744v1

27.01.2026 22:30 β€” πŸ‘ 10    πŸ” 9    πŸ’¬ 0    πŸ“Œ 0
Post image

πŸš€ CryoSPARC v5.0 BETA is here!

We’re excited to deploy another major #CryoSPARC release to help enable and accelerate #cryoEM data analysis. v5 has a redesigned underlying software system and many new features - highlights in thread!

Full changelog: cryosparc.com/updates/v5.0.0

27.01.2026 20:36 β€” πŸ‘ 63    πŸ” 31    πŸ’¬ 1    πŸ“Œ 1
Preview
Why m⁢A? An RNA surveillance model Dierks and Schwartz discuss the m6A surveillance model, proposing that m6A flags β€œundesirable” intron-less RNAs (e.g., transposons) for decay. This provides a mechanism to distinguish β€œlegitimate” spliced mRNAs and potentially suppress harmful RNA.

Online Now: Why m⁢A? An RNA surveillance model Online now:

28.01.2026 12:32 β€” πŸ‘ 14    πŸ” 11    πŸ’¬ 0    πŸ“Œ 0
Preview
Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation - Nature Communications Small regulatory RNAs can act on target mRNAs to control their translation and stability. Here, the authors present evidence that this riboregulation can potentially regulate by pairing to a target si...

Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation #rnasky 🦠

26.01.2026 12:59 β€” πŸ‘ 11    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
Preview
Polyamine sensing by nascent ornithine decarboxylase antizyme stimulates decoding of its mRNA - Nature Ornithine decarboxylase (ODC), the rate-limiting enzyme in the biosynthesis of polyamines, is regulated by an antizyme (OAZ). Polyamines induce antizyme expression by promoting ribosomal frame-shiftin...

Many many moons ago I fell in love with science while working on how Polyamines regulate programmed ribosomal frame shifting

www.nature.com/articles/nat...

Time to get back to these fascinating and complex field

24.01.2026 07:08 β€” πŸ‘ 5    πŸ” 2    πŸ’¬ 0    πŸ“Œ 0
Post image

New Preprint alert! Excited to share our latest work on the #MAPKinases from stellar PhD student Jill von Velsen. First structures of the MAP2K MEK1 activating its substrate MAPK between 2.9 and 3.6A - amazing resolutions for such a small and mobile complex! www.biorxiv.org/content/10.6...

22.01.2026 09:56 β€” πŸ‘ 21    πŸ” 8    πŸ’¬ 1    πŸ“Œ 0
Preview
A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation Abstract. Formation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) whil

And the 4th paper in this week contribution from our lab tells about ribosome biogenesis in yeast. A follow-up story from our wonderful collaborators in Graz - the Bergler Lab. Structural work was again done by the amazing @lgrundmann.bsky.social: academic.oup.com/nar/article/...

22.01.2026 17:27 β€” πŸ‘ 23    πŸ” 11    πŸ’¬ 1    πŸ“Œ 0
Post image

πŸ§ͺScientists from our Haselbach lab captured how proteins begin to fold as they’re being made.

Using cryo-EM, they visualised chaperones guiding nascent proteins on the ribosome: https://www.nature.com/articles/s41467-025-67685-6

19.01.2026 09:40 β€” πŸ‘ 50    πŸ” 16    πŸ’¬ 1    πŸ“Œ 1

We’re thrilled to share our latest iTP-seq protocol for mapping bacterial translation landscapes in vitro β€” with a complete experimental workflow streamlined by MΓ©lanie Gillard and an open source Python library for data analysis developed by Thibaud Renault.

17.01.2026 14:22 β€” πŸ‘ 12    πŸ” 9    πŸ’¬ 1    πŸ“Œ 0
Post image

Discovery and development of a new oxazolidinone with reduced toxicity for the treatment of tuberculosis @naturemedicine.bsky.social
www.nature.com/articles/s41...

15.01.2026 01:58 β€” πŸ‘ 14    πŸ” 8    πŸ’¬ 0    πŸ“Œ 0
Preview
ZAK activation at the collided ribosome | Nature Ribosome collisions activate the ribotoxic stress response mediated by the MAP3K ZAK, which in turn regulates cell-fate consequences through downstream phosphorylation of the MAPKs p38 and JNK1. Despite the critical role of ZAK during cellular stress, a mechanistic and structural understanding of ZAK–ribosome interactions and how these lead to activation remain elusive. Here we combine biochemistry and cryo-electron microscopy to discover distinct ZAK–ribosome interactions required for constitutive recruitment and for activation. We find that upon induction of ribosome collisions, interactions between ZAK and the ribosomal protein RACK1 enable its activation by dimerization of its SAM domains at the collision interface. Furthermore, we discover how this process is negatively regulated by the ribosome-binding protein SERBP1 to prevent constitutive ZAK activation. Characterization of novel SAM variants as well as a known pathogenic variant of the SAM domain of ZAK supports a key role of

Ribosome collisions activate ZAK, influencing cell fate via p38 & JNK phosphorylation. Biochemistry & cryo-EM uncover distinct ZAK-ribosome interactions. PMID:41261136, Nature 2025, @Nature https://doi.org/10.1038/s41586-025-09772-8 #Medsky #Pharmsky #RNA #ASHG #ESHG πŸ§ͺ

11.01.2026 01:10 β€” πŸ‘ 12    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
Post image

Only in Shenzhen: Science Nature coffee bar. If you’ve published in @science.org or @nature.com, they give you coffee for free. 100% real!

10.01.2026 10:41 β€” πŸ‘ 95    πŸ” 21    πŸ’¬ 16    πŸ“Œ 6
Energy-landscape model of RF2 activation. Comparison of termination complexes (TC), wild-type ArfA-bound nonstop elongation complexes (nsECs), and loss-of-function ArfA mutant-bound nsECs reveals that wild-type ArfA promotes RF2 docking to nsECs by reshaping the conformational cascade.

Energy-landscape model of RF2 activation. Comparison of termination complexes (TC), wild-type ArfA-bound nonstop elongation complexes (nsECs), and loss-of-function ArfA mutant-bound nsECs reveals that wild-type ArfA promotes RF2 docking to nsECs by reshaping the conformational cascade.

Slightly overdue article highlight!

In PNAS, we use smFRET to reveal how polypeptide release factor 2 (RF2) undergoes a cascade of structural changes to catalyze polypeptide release during translation termination and ArfA-mediated ribosome rescue.

πŸ§΅β¬‡οΈ
doi.org/10.1073/pnas...

05.01.2026 16:27 β€” πŸ‘ 19    πŸ” 11    πŸ’¬ 1    πŸ“Œ 0
Preview
Evolution of the ribosomal exit tunnel through the eyes of the nascent chain The ribosomal exit tunnel is a universally conserved feature of the large subunit that directs the nascent polypeptide chain into the cellular environment and is involved in co-translational folding, ...

Just in time for 2026! πŸŽ† Presenting a nascent-centric view on the shape of the ribosomal exit tunnel topology, based on MD-derived occupancy maps for 55 distinct ribosomes. 🧢🧬πŸ–₯️
πŸ“„ Read the preprint: biorxiv.org/content/10.6...

#StructuralBiology #Ribosome #CryoEM #Evolution #Biophysics

30.12.2025 22:30 β€” πŸ‘ 19    πŸ” 10    πŸ’¬ 0    πŸ“Œ 1
Preview
Cryo-Electron Microscopy Cold Spring Harbor Laboratory Meetings & Courses -- a private, non-profit institution with research programs in cancer, neuroscience, plant biology, genomics, bioinformatics.

Interested in learning or strengthening skills in #CryoEM single particle analysis? Apply for the CSHL cryo-EM course happening in March! This is a super intense 2 week course covering theory up through data deposition. Apps due Jan 9! Info here: meetings.cshl.edu/courses.aspx...

30.12.2025 16:16 β€” πŸ‘ 5    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
Post image

Happy Holidays from the Feaga Lab!
Strain credit to Kevin England @kevinengland.bsky.social and streaking/photo credit Katrina Callan.

25.12.2025 15:19 β€” πŸ‘ 22    πŸ” 1    πŸ’¬ 0    πŸ“Œ 0

In this study, we highlight the importance of the base composition of the first codons for protein expression. An increased abundance of adenine (A) and a decrease in guanine (G) enhance expression and improve mRNA stability. The mediator of this effect is the ribosome.

23.12.2025 10:31 β€” πŸ‘ 10    πŸ” 7    πŸ’¬ 0    πŸ“Œ 0
Post image

CryoEM folks, If you want to handle huge STAR file efficiently in Python, please try starfile-rs!

github.com/hanjinliu/star…

Reading a motion data of a particle from a 15 MB file is just like this β†“πŸ€©

23.12.2025 14:52 β€” πŸ‘ 31    πŸ” 9    πŸ’¬ 4    πŸ“Œ 0

A 1.25 A!!! cryo EM structure of rubisco.

24.12.2025 11:15 β€” πŸ‘ 23    πŸ” 9    πŸ’¬ 0    πŸ“Œ 0
Preview
Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, and...

www.biorxiv.org/content/10.6...

20.12.2025 16:38 β€” πŸ‘ 6    πŸ” 4    πŸ’¬ 0    πŸ“Œ 0
Preview
Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD NAC enables cotranslational N-terminal processing of histones H2A and H4 by recruiting MetAP1 and NatD at the ribosomal tunnel.

Last X-Mas, the ribosome gave you methionine,
but the very next day, MetAP took it away.
This year, to save histones from tears,
NatD gives you an acetyl group. ⭐️

Explore our latest paper with the Deuerling lab @uni-konstanz.de and Shu-ou Chan lab @caltech.edu!

www.science.org/doi/10.1126/...

20.12.2025 00:34 β€” πŸ‘ 46    πŸ” 17    πŸ’¬ 0    πŸ“Œ 0

@wilsonlab is following 20 prominent accounts