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TitleStructure of active dimeric human telomerase.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 4, Page 454-460, Year 2013
Publish dateMar 10, 2013
AuthorsAnselm Sauerwald / Sara Sandin / Gaël Cristofari / Sjors H W Scheres / Joachim Lingner / Daniela Rhodes /
PubMed AbstractTelomerase contains a large RNA subunit, TER, and a protein catalytic subunit, TERT. Whether telomerase functions as a monomer or dimer has been a matter of debate. Here we report biochemical and ...Telomerase contains a large RNA subunit, TER, and a protein catalytic subunit, TERT. Whether telomerase functions as a monomer or dimer has been a matter of debate. Here we report biochemical and labeling data that show that in vivo-assembled human telomerase contains two TERT subunits and binds two telomeric DNA substrates. Notably, catalytic activity requires both TERT active sites to be functional, which demonstrates that human telomerase functions as a dimer. We also present the three-dimensional structure of the active full-length human telomerase dimer, determined by single-particle EM in negative stain. Telomerase has a bilobal architecture with the two monomers linked by a flexible interface. The monomer reconstruction at 23-Å resolution and fitting of the atomic structure of the TERT subunit from beetle Tribolium castaneum into the EM density reveals the spatial relationship between RNA and protein subunits, providing insights into telomerase architecture.
External linksNat Struct Mol Biol / PubMed:23474713 / PubMed Central
MethodsEM (single particle)
Resolution23.0 - 30.0 Å
Structure data

EMDB-2310:
Three-dimensional structure of active, full-length human telomerase dimer, determined by single-particle electron microscopy in negative stain
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-2311:
Three-dimensional structure of active, full-length human telomerase. Independently refined open monomer structure, determined by single-particle electron microscopy in negative stain
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-2312:
Three-dimensional structure of active, full-length human telomerase. Independently refined closed monomer structure, determined by single-particle electron microscopy in negative stain
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Homo sapiens (human)

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