3kyl

Publication Abstract from PubMed

Telomerase is a specialized DNA polymerase that extends the 3' ends of eukaryotic linear chromosomes, a process required for genomic stability and cell viability. Here we present the crystal structure of the active Tribolium castaneum telomerase catalytic subunit, TERT, bound to an RNA-DNA hairpin designed to resemble the putative RNA-templating region and telomeric DNA. The RNA-DNA hybrid adopts a helical structure, docked in the interior cavity of the TERT ring. Contacts between the RNA template and motifs 2 and B' position the solvent-accessible RNA bases close to the enzyme active site for nucleotide binding and selectivity. Nucleic acid binding induces rigid TERT conformational changes to form a tight catalytic complex. Overall, TERT-RNA template and TERT-telomeric DNA associations are remarkably similar to those observed for retroviral reverse transcriptases, suggesting common mechanistic aspects of DNA replication between the two families of enzymes.

Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA.,Mitchell M, Gillis A, Futahashi M, Fujiwara H, Skordalakes E Nat Struct Mol Biol. 2010 Apr;17(4):513-8. Epub 2010 Mar 28. PMID:20357774^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.