Structure of active human telomerase with telomere shelterin protein TPP1.

ABSTRACT: Human telomerase is a RNA-protein complex that extends the 3' end of linear chromosomes by synthesizing multiple copies of the telomeric repeat TTAGGG¹. Its activity is a determinant of cancer progression, stem cell renewal and cellular aging^2-5. Telomerase is recruited to telomeres and activated for telomere repeat synthesis by the telomere shelterin protein TPP1^6,7. Human telomerase has a bilobal structure with a catalytic core ribonuclear protein and a H and ACA box ribonuclear protein^8,9. Here we report cryo-electron microscopy structures of human telomerase catalytic core of telomerase reverse transcriptase (TERT) and telomerase RNA (TER (also known as hTR)), and of telomerase with the shelterin protein TPP1. TPP1 forms a structured interfac

SUBMITTER: Liu B 

PROVIDER: S-EPMC9912816 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature