Summary information and primary citation
- PDB-id
-
1z31;
DSSR-derived features in text and
JSON formats
- Class
- RNA
- Method
- NMR
- Summary
- The structure of an enzyme-activating fragment of human
telomerase RNA
- Reference
-
Leeper TC, Varani G (2005): "The
structure of an enzyme-activating fragment of human
telomerase RNA." RNA, 11,
394-403. doi: 10.1261/rna.7222505.
- Abstract
- The ribonucleoprotein enzyme telomerase ensures the
stability and fidelity of linear chromosome ends by
elongating the telomeric DNA that is lost during each round
of DNA replication. All telomerases contain a catalytic
protein component homologous to viral reverse
transcriptases (TERT) and an RNA (TR) that provides the
template sequence, acts as the scaffold for
ribonucleoprotein assembly, and activates the enzyme for
catalysis. Vertebrate telomerase RNAs contain three highly
conserved structural and functional domains: the template
domain, the "CR4-CR5" or "activation" domain essential for
activation of the enzymatic activity, and a 3'-terminal
"box H/ACA"-homology domain responsible for
ribonucleprotein assembly and maturation. Here we report
the NMR structure of a functionally essential RNA
structural element derived from the human telomerase RNA
CR4-CR5 domain. This RNA, referred to as hTR J6, forms a
stable hairpin interrupted by a single nucleotide bulge and
an asymmetric internal loop. Previous work on telomerase
has shown that deletion of the hTR J6 asymmetric internal
loop results in an RNA incapable of binding the enzymatic
protein component of the RNP and therefore an inactive RNP
without telomerase activity. We demonstrate here that the
J6 internal loop introduces a twist in the RNA structure
that may position the entire domain into the catalytic site
of the enzyme.
