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Exploring real-time interaction analysis to monitor CD44 expression modulation in cancer cells by inhibiting Musashi-1 interactions with RNA
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Biokemi.ORCID-id: 0000-0001-7595-4851
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för kirurgiska vetenskaper, Öron-, näs- och halssjukdomar. Uppsala universitet, Science for Life Laboratory, SciLifeLab. Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Cancerprecisionsmedicin.ORCID-id: 0000-0003-4662-3142
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Biokemi. Uppsala universitet, Science for Life Laboratory, SciLifeLab.ORCID-id: 0000-0003-2728-0340
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(engelsk)Manuskript (preprint) (Annet vitenskapelig)
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Identifikatorer
URN: urn:nbn:se:uu:diva-552063OAI: oai:DiVA.org:uu-552063DiVA, id: diva2:1942887
Tilgjengelig fra: 2025-03-06 Laget: 2025-03-06 Sist oppdatert: 2025-03-06
Inngår i avhandling
1. Insights into Musashi-1 interactions with RNA: From in vitro kinetics to cell biology
Åpne denne publikasjonen i ny fane eller vindu >>Insights into Musashi-1 interactions with RNA: From in vitro kinetics to cell biology
2025 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

The interaction between proteins and RNA has gained increased attention as a key regulatory mechanism of RNA translation beyond conventional postulated mechanisms. It is also involved in various pathologies, including cancer and neurodegenerative disorders. In this thesis, the interactions between the RNA-binding protein Musashi-1 (MSI1) and both linear and hairpin-like RNA strands have been investigated using time-resolved and structural technologies, such as SPR biosensors, LigandTracer, and NMR.

Initially, the interactions of the two RNA recognition motifs (RRM1 and RRM2) in MSI1 were characterized separately. Both motifs exhibited high affinity for the UAG motif, with no significant difference between linear and hairpin-like RNA. These interactions followed a 1:1 binding mechanism, with relatively fast, but well-defined association and dissociation rate constants. Next, the interaction of the N-terminal region of MSI1, containing both RRMs, was analyzed, revealing a bivalent binding mechanism. Commercial software was not suitable for distinguishing the fast monovalent and slow bivalent interactions. Therefore, a novel method was developed to quantify kinetic rate constants and binding affinities.

To explore the determinants for the specificity of the interaction, RNA mutants and protein variants were designed to shift RRM2 recognition from the UAG to the CAG motifs. Comprehensive characterization confirmed the impact of these mutations and RNA structural modifications on the interaction.

Additionally, to examine MSI1 regulatory role in synthetic biology, a post-transcriptionally controlled circuit was engineered in E. coli using MSI1 binding to RNA strands. This system, developed on solid media, utilized sfGFP fluorescence as a reporter. Data analysis using the Gompertz growth model correlated well with previously published data on bacteria in suspension. The regulatory effect of oleic acid, a potential MSI1 allosteric inhibitor, was confirmed using this assay. Similarly, MSI1 inhibition effects were assessed in HCT-116 colorectal cancer cells, revealing that both oleic acid and luteolin impacted cell proliferation and CD44v6 receptor expression.

In conclusion, this work has resulted in novel methods and insights for studying and understanding the kinetics and mechanisms of protein-RNA interactions.

sted, utgiver, år, opplag, sider
Uppsala: Acta Universitatis Upsaliensis, 2025. s. 78
Serie
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 2508
Emneord
Interaction kinetics, biochemistry, RNA-protein interactions, RNA binding proteins, synthetic biology
HSV kategori
Forskningsprogram
Biokemi
Identifikatorer
urn:nbn:se:uu:diva-552069 (URN)978-91-513-2408-1 (ISBN)
Disputas
2025-04-25, A1:107, BMC, Husargatan 3, Uppsala, 09:00 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2025-04-02 Laget: 2025-03-06 Sist oppdatert: 2025-04-02

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