Structural biology of telomerase and its interaction at telomeres. Curr Opin Struct Biol 2017 Dec;47:77-87
Date
07/22/2017Pubmed ID
28732250Pubmed Central ID
PMC5564310DOI
10.1016/j.sbi.2017.06.010Scopus ID
2-s2.0-85024400278 (requires institutional sign-in at Scopus site) 27 CitationsAbstract
Telomerase is an RNP that synthesizes the 3' ends of linear chromosomes and is an important regulator of telomere length. It contains a single long non-coding telomerase RNA (TER), telomerase reverse transcriptase (TERT), and other proteins that vary among organisms. Recent progress in structural biology of telomerase includes reports of the first cryo-electron microscopy structure of telomerase, from Tetrahymena, new crystal structures of TERT domains, telomerase RNA structures and models, and identification in Tetrahymena telomerase holoenzyme of human homologues of telomere-associated proteins that have provided a more unified view of telomerase interaction at telomeres as well as insights into the role of telomerase RNA in activity and assembly.
Author List
Wang Y, Feigon JAuthor
Yaqiang Wang PhD, MS Assistant Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Cryoelectron MicroscopyModels, Biological
Models, Molecular
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Structure-Activity Relationship
Telomerase
Telomere
