All Outputs (15)

Determining the effects of pseudouridine incorporation on human tRNAs (2025)
Journal Article
Biela, A. D., Nowak, J. S., Biela, A. P., Mukherjee, S., Moafinejad, S. N., Maiti, S., Chramiec-Głąbik, A., Mehta, R., Jeżowski, J., Dobosz, D., Dahate, P., Arluison, V., Wien, F., Indyka, P., Rawski, M., Bujnicki, J. M., Lin, T.-Y., & Glatt, S. (online). Determining the effects of pseudouridine incorporation on human tRNAs. The EMBO Journal, https://doi.org/10.1038/s44318-025-00443-y

Transfer RNAs (tRNAs) are ubiquitous non-coding RNA molecules required to translate mRNA-encoded sequence information into nascent polypeptide chains. Their relatively small size and heterogenous patterns of their RNA modifications have impeded the s... Read More about Determining the effects of pseudouridine incorporation on human tRNAs.

The molecular basis of tRNA selectivity by human pseudouridine synthase 3 (2024)
Journal Article
Lin, T.-Y., Kleemann, L., Jezowski, J., Dobosz, D., Rawski, M., Indyka, P., Wazny, G., Mehta, R., Chramiec-Glabik, A., Koziej, L., Ranff, T., Fufezan, C., Wawro, M., Kochan, J., Bereta, J., A. Leidel, S., & Glatt, S. (2024). The molecular basis of tRNA selectivity by human pseudouridine synthase 3. Molecular Cell, 84(13), 2472-2489.e8. https://doi.org/10.1016/j.molcel.2024.06.013

Pseudouridine (Ψ), the isomer of uridine, is ubiquitously found in RNA, including tRNA, rRNA, and mRNA. Human pseudouridine synthase 3 (PUS3) catalyzes pseudouridylation of position 38/39 in tRNAs. However, the molecular mechanisms by which it recogn... Read More about The molecular basis of tRNA selectivity by human pseudouridine synthase 3.

Cryo-EM structures of the human Elongator complex at work (2024)
Journal Article
Abbassi, N., Jaciuk, M., Scherf, D., Böhnert, P., Rau, A., Hammermeister, A., …Glatt, S. (2024). Cryo-EM structures of the human Elongator complex at work. Nature Communications, 15(1), Article 4094. https://doi.org/10.1038/s41467-024-48251-y

tRNA modifications affect ribosomal elongation speed and co-translational folding dynamics. The Elongator complex is responsible for introducing 5-carboxymethyl at wobble uridine bases (cm5U34) in eukaryotic tRNAs. However, the structure and function... Read More about Cryo-EM structures of the human Elongator complex at work.

Electrophoretic Mobility Shift Assay (EMSA) and Microscale Thermophoresis (MST) Methods to Measure Interactions Between tRNAs and Their Modifying Enzymes (2023)
Book Chapter
Chramiec-Głąbik, A., Rawski, M., Glatt, S., & Lin, T. (2023). Electrophoretic Mobility Shift Assay (EMSA) and Microscale Thermophoresis (MST) Methods to Measure Interactions Between tRNAs and Their Modifying Enzymes. . Springer US. https://doi.org/10.1007/978-1-0716-3191-1_3

Cryo-EM structure of the fully assembled Elongator complex (2023)
Journal Article
Jaciuk, M., Scherf, D., Kaszuba, K., Gaik, M., Rau, A., Kościelniak, A., …Glatt, S. (2023). Cryo-EM structure of the fully assembled Elongator complex. Nucleic Acids Research, 51(5), 2011-2032. https://doi.org/10.1093/nar/gkac1232

Transfer RNA (tRNA) molecules are essential to decode messenger RNA codons during protein synthesis. All known tRNAs are heavily modified at multiple positions through post-transcriptional addition of chemical groups. Modifications in the tRNA antico... Read More about Cryo-EM structure of the fully assembled Elongator complex.

Destabilization of mutated human PUS3 protein causes intellectual disability (2022)
Journal Article
Lin, T., Smigiel, R., Kuzniewska, B., Chmielewska, J. J., Kosińska, J., Biela, M., …Glatt, S. (2022). Destabilization of mutated human PUS3 protein causes intellectual disability. Human Mutation: Variation, Informatics and Disease, 43(12), 2063-2078. https://doi.org/10.1002/humu.24471

Pseudouridine (Ψ) is an RNA base modification ubiquitously found in many types of RNAs. In humans, the isomerization of uridine is catalyzed by different stand-alone pseudouridine synthases (PUS). Genomic mutations in the human pseudouridine synthase... Read More about Destabilization of mutated human PUS3 protein causes intellectual disability.

ACEing premature codon termination using anticodon-engineered sup-tRNA-based therapy (2022)
Journal Article
Lin, T., & Glatt, S. (2022). ACEing premature codon termination using anticodon-engineered sup-tRNA-based therapy. Molecular Therapy - Nucleic Acids, 29, 368-369. https://doi.org/10.1016/j.omtn.2022.07.019

Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B (2021)
Journal Article
Pakosz, Z., Lin, T., Michalczyk, E., Nagano, S., & Heddle, J. G. (2021). Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B. Antimicrobial Agents and Chemotherapy, 65(10), https://doi.org/10.1128/aac.00267-21

Malaria persists as a major health problem due to the spread of drug resistance and the lack of effective vaccines. DNA gyrase is a well-validated and extremely effective therapeutic target in bacteria, and it is also known to be present in the apico... Read More about Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B.

Pseudouridines in RNAs: switching atoms means shifting paradigms (2021)
Journal Article
Lin, T., Mehta, R., & Glatt, S. (2021). Pseudouridines in RNAs: switching atoms means shifting paradigms. FEBS Letters, 595(18), 2310-2322. https://doi.org/10.1002/1873-3468.14188

The structure, stability, and function of various coding and noncoding RNAs are influenced by chemical modifications. Pseudouridine (Ψ) is one of the most abundant post-transcriptional RNA base modifications and has been detected at individual positi... Read More about Pseudouridines in RNAs: switching atoms means shifting paradigms.

How Elongator Acetylates tRNA Bases (2020)
Journal Article
Abbassi, N., Biela, A., Glatt, S., & Lin, T. (2020). How Elongator Acetylates tRNA Bases. International Journal of Molecular Sciences, 21(21), 8209. https://doi.org/10.3390/ijms21218209

Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U34) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects... Read More about How Elongator Acetylates tRNA Bases.

Enzyme encapsulation by protein cages (2020)
Journal Article
Chakraborti, S., Lin, T., Glatt, S., & Heddle, J. G. (2020). Enzyme encapsulation by protein cages. RSC Advances, 10(22), 13293-13301. https://doi.org/10.1039/c9ra10983h

Protein cages are hollow protein shells with a nanometric cavity that can be filled with useful materials. The encapsulating nature of the cages means that they are particularly attractive for loading with biological macromolecules, affording the gue... Read More about Enzyme encapsulation by protein cages.

Molecular basis of tRNA recognition by the Elongator complex (2019)
Journal Article
Dauden, M. I., Jaciuk, M., Weis, F., Lin, T., Kleindienst, C., Abbassi, N. E. H., …Glatt, S. (2019). Molecular basis of tRNA recognition by the Elongator complex. Science Advances, 5(7), https://doi.org/10.1126/sciadv.aaw2326

The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain... Read More about Molecular basis of tRNA recognition by the Elongator complex.

The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase (2019)
Journal Article
Lin, T., Abbassi, N. E. H., Zakrzewski, K., Chramiec-Głąbik, A., Jemioła-Rzemińska, M., Różycki, J., & Glatt, S. (2019). The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase. Nature Communications, 10(1), https://doi.org/10.1038/s41467-019-08579-2

The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm5) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a... Read More about The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.

Liquid Crystalline Granules Align in a Hierarchical Structure To Produce Spider Dragline Microfibrils (2017)
Journal Article
Lin, T., Masunaga, H., Sato, R., Malay, A. D., Toyooka, K., Hikima, T., & Numata, K. (2017). Liquid Crystalline Granules Align in a Hierarchical Structure To Produce Spider Dragline Microfibrils. Biomacromolecules, 18(4), 1350-1355. https://doi.org/10.1021/acs.biomac.7b00086

Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi (2016)
Journal Article
Glatt, S., Zabel, R., Kolaj-Robin, O., Onuma, O. F., Baudin, F., Graziadei, A., …Müller, C. W. (2016). Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi. Nature Structural and Molecular Biology, 23(9), 794-802. https://doi.org/10.1038/nsmb.3265

During translation elongation, decoding is based on the recognition of codons by corresponding tRNA anticodon triplets. Molecular mechanisms that regulate global protein synthesis via specific base modifications in tRNA anticodons are receiving incre... Read More about Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.