{"id":451,"date":"2026-05-05T15:58:43","date_gmt":"2026-05-05T13:58:43","guid":{"rendered":"https:\/\/webs.uab.cat\/rna-rnase\/?page_id=451"},"modified":"2026-07-07T09:35:13","modified_gmt":"2026-07-07T07:35:13","slug":"summer-seminar-2026","status":"publish","type":"page","link":"https:\/\/webs.uab.cat\/rna-rnase\/summer-seminar-2026\/","title":{"rendered":"Summer Seminar 2026"},"content":{"rendered":"\n

14th July 2026<\/h1>\n\n\n\n
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09:00-09:30 (CET)<\/p>\n\n\n\n

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Dr. Uciel Chorostecki<\/strong><\/strong><\/p>\n<\/blockquote>\n\n\n\n

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Faculty of Medicine and Health Sciences, <\/p>\n\n\n\n

Department of Biomedical Sciences, <\/p>\n\n\n\n

Universitat Internacional de Catalunya<\/p>\n<\/div>\n\n\n\n

<\/a>Computational RNA Biology Lab<\/a><\/strong><\/p>\n\n\n\n

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More details<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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09:30-10:00 (CET)<\/p>\n\n\n\n

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Dr. Lin Huang<\/strong><\/strong><\/p>\n<\/blockquote>\n\n\n\n

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Sun Yat-sen Memorial Hospital,<\/p>\n\n\n\n

Sun Yat-sen University<\/p>\n<\/div>\n\n\n\n

Nucleic Acid Structure Research Group<\/a><\/strong><\/strong><\/strong><\/p>\n\n\n\n

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More details<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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10:00-10:30 (CET)<\/p>\n\n\n\n

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Dr. Markus H\u00f6pfler<\/strong><\/p>\n<\/blockquote>\n\n\n\n

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Centre de Regulaci\u00f3 Gen\u00f2mica <\/p>\n\n\n\n

(CRG)<\/p>\n<\/div>\n\n\n\n

Dynamics of protein synthesis & RNA decay<\/a><\/strong><\/strong><\/p>\n\n\n\n

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More details<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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10:45-11:15 (CET)<\/p>\n\n\n\n

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Dr. Roeland Boer<\/strong><\/p>\n<\/blockquote>\n\n\n\n

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XALOC Beamline,<\/p>\n\n\n\n

ALBA Synchrotron, Spain<\/p>\n<\/div>\n\n\n\n

BL13 \u2013 XALOC \u2013 ALBA Synchrotron<\/a><\/strong><\/strong><\/p>\n\n\n\n

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More details<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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11:15-11:45 (CET)<\/p>\n\n\n\n

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Xincheng Kang\/Dr.<\/strong><\/strong> Guillem Prats-Ejarque<\/strong><\/p>\n<\/blockquote>\n\n\n\n

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Departament de Bioqu\u00edmica i Biologia Molecular, <\/p>\n\n\n\n

Universitat Aut\u00f2noma de Barcelona<\/p>\n<\/div>\n\n\n\n

Human Ribonucleases involved in host defence<\/a><\/strong><\/p>\n\n\n\n

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More details<\/a><\/div>\n<\/div>\n<\/div>\n<\/div>\n\n\n\n
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Time: 09:00-09:30_Dr. Uciel Chorostecki<\/strong><\/strong><\/strong><\/strong><\/strong><\/h1>\n<\/blockquote>\n\n\n\n
Predicting RNA Structure- function relationship<\/strong><\/strong><\/summary>
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<\/p>\n<\/div><\/details>\n\n\n\n

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Time: 09:30-10:00_Dr. <\/strong>Lin<\/strong><\/strong> Huang<\/strong><\/strong><\/h1>\n<\/blockquote>\n\n\n\n
Data-Driven Nucleic Acid Crystallography<\/strong><\/summary>
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The three-dimensional structures of functional nucleic acids (RNA\/DNA) are the key to understanding their functions, designing targeted drugs, and developing synthetic-biology components. However, the low efficiency of nucleic acid crystallization and the long cycle required for phase determination remain the central bottlenecks constraining this field. We are committed to transforming empirical knowledge into standardized methods and further developing these methods into automated tools, thereby advancing nucleic acid crystallography into a new stage.<\/p>\n\n\n\n

Database Development<\/p>\n\n\n\n

\u2022 Based on the three established data platforms Ribocentre1<\/sup> (ribozymes), Ribocentre-switch2<\/sup> (riboswitches), and Ribocentre-aptamer3<\/sup> (aptamers), we are integrating 50 years of worldwide RNA crystallography data to build the first RNA crystallization methodology database (unpublished).<\/p>\n\n\n\n

Two Original Technologies<\/p>\n\n\n\n

\u2022 GU base-pair engineering: By introducing or removing GU base pairs, we have successfully determined 10 RNA crystal structures4,5,6<\/sup>.<\/p>\n\n\n\n

\u2022 The counterintuitive \u201cextension of nonfunctional stems\u201d paradigm: Statistical analysis shows that nonfunctional stem regions in nucleic acids are typically 4\u20138 base pairs (bp) long. Extending them to 9\u201312 bp can both increase the probability of crystallization and intrinsically provide a molecular-replacement search model. This strategy has successfully enabled the determination of multiple new functional nucleic acid structures (unpublished).<\/p>\n\n\n\n

Finally, I will also discuss which interesting structures we have determined using these efficient methods, what new insights these structures have generated, and what scientific questions they have helped address7,8,9,10<\/sup>.<\/p>\n\n\n\n

Keywords: crystallography; nucleic acids; ribozymes; riboswitches; aptamers<\/p>\n\n\n\n

References<\/p>\n\n\n\n

[1] Deng, J\u2026 Huang, L. Nucleic Acids Research. 2023, 51, D262\u2013D268.<\/p>\n\n\n\n

[2] Bu, F.; \u2026 Huang, L. Nucleic Acids Research 2024, 52, D265\u2013D272.<\/p>\n\n\n\n

[3] Lu, Z.; \u2026 Huang, L.; Miao, Z. Nucleic Acids Research 2026, 54, D264\u2013D272.<\/p>\n\n\n\n

[4] Ren, Y.; \u2026 Huang, L. Nucleic Acids Research 2025, 53 (3), gkae1218.<\/p>\n\n\n\n

[5] He, Y.; \u2026 Huang, L. Cell Discovery 2025, 10 (1), 128.<\/p>\n\n\n\n

[6] Chen, K.; \u2026 Huang, L. Nucleic Acids Research 2025, 53 (14), gkaf702.<\/p>\n\n\n\n

[7] Deng, J\u2026 Huang, L. Nature Chemical Biology 2022, 18 (5), 556\u2013564.<\/p>\n\n\n\n

[8] He, Y.; \u2026 Huang, L. Nucleic Acids Research 2026, 54 (6), gkag211.<\/p>\n\n\n\n

[9] Lin, X.; \u2026 Huang, L. Angewandte Chemie 2025, 137 (22).<\/p>\n\n\n\n

[10] Wang, J.; \u2026 Huang, L.; Tan, J. Chem 2026, 12 (5), 102883.<\/p>\n<\/div><\/details>\n\n\n\n

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Time: 10:00-10:30_Dr. Markus H\u00f6pfler<\/strong><\/strong><\/strong><\/h1>\n<\/blockquote>\n\n\n\n
Mechanism and regulation of selective tubulin mRNA degradation<\/strong><\/summary>
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In the \u201cDynamics of protein synthesis & RNA decay\u201d lab we are interested in how cells tune protein production by adjusting the stability of messenger RNAs (mRNAs). Each cell in our body expresses around 12,000 different mRNAs at any given time. To control this complex transcriptome\u2014and thus protein synthesis\u2014cells adjust half-lives for individual mRNAs from minutes to several days. Traditionally, the selective degradation of mRNAs has been attributed to the recognition of nucleotide sequence elements by proteins or small RNAs that subsequently recruit decay factors. In our lab, we investigate a distinct, newly emerging paradigm of gene regulation termed \u201cpeptide-mediated mRNA decay\u201d (PMD). In PMD, not the mRNA sequence but rather the nascent protein is recognized to trigger degradation of the encoding mRNA during its translation by the ribosome.<\/p>\n\n\n\n

This process is exemplified by tubulin mRNAs: Microtubules, built from heterodimers of alpha- and beta-tubulins, control cell shape, mediate intracellular transport and power cell division. The concentration of tubulins is tightly controlled through a post-transcriptional mechanism involving selective and regulated degradation of tubulin-encoding mRNAs. We and others recently demonstrated that degradation is initiated by TTC5, which recognizes tubulin-synthesizing ribosomes and recruits the downstream effectors SCAPER and CCR4-NOT to trigger mRNA decay (Lin et al., 2020, Science<\/em>; H\u00f6pfler et al., 2023, Mol Cell<\/em>). Subsequently, we identified the first regulatory step of this cascade that controls TTC5 activity (Batiuk, H\u00f6pfler, et al., 2024, Nat Commun<\/em>). Together, our data provide a conceptual framework for peptide-mediated mRNA decay. Building on this, future work will investigate how PMD globally shapes the human transcriptome.<\/p>\n<\/div><\/details>\n\n\n\n

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Time: 10:45-11:15_Dr. Roeland Boer<\/strong><\/strong><\/strong><\/h1>\n<\/blockquote>\n\n\n\n
Macromolecular crystallography tools to study protein-nucleic acid complexes<\/strong><\/summary>
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Time: 11:15-11:45_Xincheng Kang\/Dr.<\/strong><\/strong> Guillem Prats-Ejarque<\/strong><\/strong><\/h1>\n<\/blockquote>\n\n\n\n
Crystallographic screening of an RNase for structure-based drug design<\/strong><\/summary>
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Human RNase 2, also named the eosinophil-derived neurotoxin (EDN), is a secretory protein of the vertebrate-specific RNase A superfamily involved in antiviral and proinflammatory cell response. Identifying ligand-binding pockets in EDN is thus relevant to structure-based drug design. By X-ray crystallography we first identified a conserved site at the protein surface binding to carboxylic anion molecules: malonate, tartrate and citrate. Searching for potential biomolecules rich in anion groups and considering previous report of EDN interaction to glycosaminoglycans, we explored the protein binding to saccharides. EDN crystals were soaked with mono- and disaccharides, and the 3D structures of ten complexes were solved by X-ray crystallography at atomic resolution. We identified protein binding sites to glucose, fucose, mannose, galactose, trehalose, sucrose, N-acetyl-D-glucosamine, N-acetylmuramic acid, and the sialic acid N-acetylneuraminic acid. A main site for glucose, fucose, and galactose was located adjacent to the spotted carboxylic anion site. Secondarily, N-acetylneuraminic acid and mannose shared another close by protein surface region. Overall, we located 17 saccharide ligands that clustered into seven defined sites, outlining a conserved recognition pattern, which was further analysed by molecular modelling. Interestingly, within the RNase A superfamily, we find amphibian RNases that were initially isolated as carbohydrate binding proteins and named as leczymes, combining enzymatic and lectin properties. The present data is the first structural characterization of a mammalian sugar-binding RNase within the family. The results highlight unique EDN residues that mediate sugar specific interactions, of particular interest for a better understanding of the protein physiological role.<\/p>\n<\/div><\/details>\n<\/div>\n\n\n\n

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Free Registration<\/strong><\/p>https:\/\/forms.office.com\/e\/g4q1Qry521<\/a><\/cite><\/blockquote><\/figure>\n\n\n\n

Teams link for the event<\/strong><\/p>14th,July, 2026<\/cite><\/blockquote><\/figure>\n\n\n\n

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teams<\/a><\/div>\n<\/div>\n\n\n\n
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10:30-10:45 Break<\/strong><\/p>\n<\/blockquote>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"

14th July 2026 09:00-09:30 (CET) Dr. Uciel Chorostecki Faculty of Medicine and Health Sciences, Department of Biomedical Sciences, Universitat Internacional de Catalunya Computational RNA Biology Lab 09:30-10:00 (CET) Dr. Lin Huang Sun Yat-sen Memorial Hospital, Sun Yat-sen University Nucleic Acid Structure Research Group 10:00-10:30 (CET) Dr. Markus H\u00f6pfler Centre de Regulaci\u00f3 Gen\u00f2mica (CRG) Dynamics of […]<\/p>\n","protected":false},"author":2988,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-451","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/pages\/451","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/users\/2988"}],"replies":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/comments?post=451"}],"version-history":[{"count":48,"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/pages\/451\/revisions"}],"predecessor-version":[{"id":519,"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/pages\/451\/revisions\/519"}],"wp:attachment":[{"href":"https:\/\/webs.uab.cat\/rna-rnase\/wp-json\/wp\/v2\/media?parent=451"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}