Progress in structural studies of telomerase

Curr Opin Struct Biol. 2014 Feb:24:115-24. doi: 10.1016/j.sbi.2014.01.008. Epub 2014 Feb 4.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Humans
  • Models, Molecular
  • Protein Multimerization
  • Telomerase / chemistry*
  • Telomerase / metabolism
  • Tetrahymena thermophila / chemistry
  • Tetrahymena thermophila / enzymology

Substances

  • Telomerase