title: Progress in structural studies of telomerase.
abstract: Telomerase is the ribonucleoprotein (RNP) reverse transcriptase responsible for synthesizing the 3' ends of linear chromosomes. It plays critical roles in tumorigenesis, cellular aging, and stem cell renewal. The past two years have seen exciting progress in determining telomerase holoenzyme architecture and the structural basis of telomerase activity. Notably, the first electron microscopy structures of telomerase were reported, of the Tetrahymena thermophila telomerase holoenzyme and a human telomerase dimer. In addition to new structures of TERT and TER domains, the first structures of telomerase protein domains beyond TERT, and their complexes with TER or telomeric single-stranded DNA, were reported. Together these studies provide the first glimpse into the organization of the proteins and RNA in the telomerase RNP.
authors: Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA.
authors: Edward J
authors: EJ
authors: Miracco
authors: Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA; Department of Microbiology, Immunology and Molecular Genetics, University of California Los Angeles, Los Angeles, CA 90095, USA; California Nanosystems Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.
authors: Jiansen
authors: J
authors: Jiang
authors: Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA.
authors: Darian D
authors: DD
authors: Cash
authors: Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA; California Nanosystems Institute, University of California Los Angeles, Los Angeles, CA 90095, USA. Electronic address: feigon@mbi.ucla.edu.
authors: Juli
authors: J
authors: Feigon
mesh_terms: D000818:Animals; D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization; D019098:Telomerase / Q000737:chemistry* / Q000378:metabolism; D016808:Tetrahymena thermophila / Q000737:chemistry / Q000201:enzymology
chemical_list: D019098:Telomerase