ASCC1 structures and bioinformatics reveal a novel helix-clasp-helix RNA-binding motif linked to a two-histidine phosphodiesterase
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Biochemistry & Molecular Biology↗
Engineering topics
Thapar, Roopa
Publications and source records attributed to Thapar, Roopa.
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM
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59 BASIC BIOLOGICAL SCIENCES↗
Mechanism of efficient double-strand break repair by a long non-coding RNA
The Authors wish to correct an error in Figure 6. In Figure 6B the panel label should read ‘Ku + DNA-PKcs + LINP1, 6 kbp bridge’ instead of ‘Ku + DNA-PKcs + PAXX, 6 kbp bridge’. The published article has been updated. This error does not affect the conclusions of the article.
59 BASIC BIOLOGICAL SCIENCES↗
Mechanism of efficient double-strand break repair by a long non-coding RNA
Mechanistic studies in DNA repair have focused on roles of multi-protein DNA complexes, so how long non-coding RNAs (lncRNAs) regulate DNA repair is less well understood. Yet, lncRNA LINP1 is over-expressed in multiple cancers and confers resistance to ionizing radiation and chemotherapeutic drugs. Here, we unveil structural and mechanistic insights into LINP1’s ability to facilitate non-homologous end joining (NHEJ). We characterized LINP1 structure and flexibility and analyzed interactions with the NHEJ factor Ku70/Ku80 (Ku) and Ku complexes that direct NHEJ. LINP1 self-assembles into phase-separated condensates via RNA–RNA interactions that reorganize to form filamentous Ku-containing aggregates. Structured motifs in LINP1 bind Ku, promoting Ku multimerization and stabilization of the initial synaptic event for NHEJ. Significantly, LINP1 acts as an effective proxy for PAXX. Collective results reveal how lncRNA effectively replaces a DNA repair protein for efficient NHEJ with implications for development of resistance to cancer therapy.
59 BASIC BIOLOGICAL SCIENCES↗