T. R. Cech

This study identifies a misfolded CR4/5 conformation in hTR that is not required for hTERT binding and is detrimental to telomerase activity.

The paper presents a cryo-EM structure of PRC2 bound to G-quadruplex RNA, revealing how RNA inhibits PRC2 by promoting dimerization and blocking DNA interaction.

The paper demonstrates that RNA- and DNA-binding proteins can directly transfer polynucleotides, enabling one-dimensional target site search and suggesting regulated complex lifetimes in vivo.

This study reveals a direct transfer mechanism by which PRC2 exchanges RNA and DNA/nucleosome in its binding site, reconciling conflicting in vitro and in vivo findings on RNA's role in regulating PRC2 activity.

This study shows that DNMT1 interacts with pUG-fold RNA, which inhibits its activity by blocking DNA binding.

The paper investigates CST's role in telomerase inhibition and shows it does not terminate ongoing telomerase extension but prevents initiation through ssDNA binding.

The paper shows that intron retention drives nuclear compartmentalization of TERT mRNA and TUG1 lncRNA, impacting cell growth and suggesting new RNA-based therapy targets.

The paper reports the cryo-EM structure of human CST bound to telomeric DNA, revealing a decameric supercomplex and providing insights into CST function and disease associations.

The paper uses single-molecule RNA FISH to analyze TERT expression in cancer cell lines, revealing cell-to-cell variation, complex gene expression patterns, and unexpected nuclear localization of TERT mRNA.

This study identifies EZH2 automethylation as a regulatory mechanism that modulates PRC2 histone methyltransferase activity.

This study uses live-cell imaging to show that telomerase recruitment depends on DNA base-pairing and processivity in human cells.