Niels Fischer
@N__Fischer
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Project group leader in structural biology @mpi_nat
Joined June 2021
How does the human #ribosome machinery select an open reading frame on mRNA for translation? Check out our #cryoEM work @NatureSMB: https://t.co/GC2xgcMcez Thanks to all involved - most of all first author @V_Petrychenko and our collaborators from the Rodnina lab @mpi_nat. 1/5
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Our latest work is out in @Nature today! Using smFRET, we directly visualized recruitment of the eIF4F complex to the 5' cap of eukaryotic mRNAs and formation of an activated mRNA. Our findings reveal new and surprising roles for each eIF4F component. 1/3 https://t.co/THosKn33fC
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Happy to share our little discovery with @SimoneMattei19 team on how ribosomes hibernate upside down on mitochondria during cellular stress is now out @NatureComms! A collaboration between @medicineUVA, @EMBL, @EmblImaging, MEMC. Congrats to all authors! https://t.co/DE6eAamt5I
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Ever wondered what else to do with your 3D printer? Here we used it to simulate #ribosome subunit joining in presence of the large eIF3 complex. Read our full #cryoEM story on the human 48S translation initiation machinery @Naturesmb: https://t.co/Ye0Der1UA5
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Strikingly, we find that eIF3 senses the 48S state to control subunit joining, triggering release of the eIF3c-NTD from the 40S at the final stage to enable 60S docking. These findings also explain how eIF3 could function in context of the 80S ribosome. 5/5
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Upon GTP hydrolysis, eIF2 releases the initiator tRNA & becomes highly dynamic, making way for eIF5B and tRNA transfer to eIF5B, initiating release of eIF5 and eIF2. These key commitment steps finalize start site selection & remodel the 48S for subunit joining. 4/5
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The structures visualize the process of start site selection in unprecedented detail and clarify the structural role of the mRNA Kozak sequence in regulating translation efficiency by facilitating mRNA scanning and stabilizing 40S closure. 3/5
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Our cryo-EM snapshots resolve the entire pathway by which the human 48S translation initiation complex (48S) selects an ORF – from the initial start site search and large-scale remodeling to the last step ready for joining of ribosomal subunits. 2/5
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Last week my main project was published at @NatureComms, so there is a thread about our findings: https://t.co/ETbrP24DUT
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Our new paper is finally out! We discovered that the human tumor suppressor protein Pdcd4 binds to the #mRNA entry channel in the 40S ribosomal subunit, where it blocks the eIF4F-independent role of eIF4A. #ribosome #CryoEM @umichrna @UMLifeSciences
https://t.co/IyJSmzXgXg
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Great work and movie on the structure and function of eIF4A and eIF4F in the human 48S translation initiation complex, congrats!
I am thrilled to share our new paper published in @NatureSMB (Brito Querido et al., 2024). #CryoEM structure of a human translation initiation complex reveals two independent roles for the helicase eIF4A. #Ribosome #mRNA #Science
https://t.co/3g4mNiw88j
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I am thrilled to share our manuscript published in @NatRevMCB. In this Review (Brito Querido et al., 2023), we discuss the current state of knowledge on eukaryotic translation initiation and its regulation in health and disease.
Now Online The molecular basis of translation initiation and its regulation in eukaryotes https://t.co/QRvvqPfzhP
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It has been really a pleasure to participate in the summer school of the @Tampe_Lab and give a talk on the human #ribosome & atomic-resolution #cryoEM. Big thanks to Robert Tampé, the whole Tampé lab, Anne Halenius & @BosnjakBerislav for great scientific tales and discussions!
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Collaboration of Tatyana Pestova & @joachimfrank labs @Columbia @sunydownstate reveals the molecular architecture of 40S translation initiation complexes on hepatitis C virus #HCV #IRES by #cryoEM
https://t.co/6T4Ro9PHeF
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Today, our work in partnership with @shsternberg lab is published: https://t.co/M7AvGR8Hcv Amazing (and hard) journey with @fthoffmann @JingWang0610 Leslie, MinJoo and more! Thanks to all for your hard work and 👇 a taste of what we saw.
nature.com
Nature - CRISPR-associated transposons exploit a proofreading checkpoint to ensure high-fidelity selection of genomic sites for DNA insertion through specific recruitment of TnsC oligomers by the...
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It's been a pleasure to present our new data on the structural dynamics of human translation initiation on the fantastic @2022Ribosomes conference. Big thanks to @Hashemyaser4, @InnisLab & @IgnatovaLab for organizing this amazing meeting.
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Fantastic PI & great scientific environment. Postdocs join! Congrats, Jailson.
I’m thrilled to share that I will be leaving the Ramakrishnan Lab at the @MRC_LMB to start my lab at Michigan Medical School this fall. I’m really looking forward to joining the UM as an Asst. Professor, RNA Scholar of the @umichrna, and BSSP Scholar. #UMBiosciences #RNA #CryoEM
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If you are interested in joining the vibrant cryo-EM community in Bordeaux (@fronzes_lab, @Hashemyaser4, Nicolas Reyes, @krastevalab, @InnisLab...), please apply to the 2022 IECB call for new group leaders. Deadline June 15! (2/2) https://t.co/R8l4uhoQ74
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Congratulations to Marina Rodnina on becoming an International Member of @theNASciences.🥂 The U.S. academy honors her for her innovative #research on the structure and function of #ribosomes – the protein factories of living #cells. https://t.co/rpZmQCku8E
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