Structural highlights
Function
TAP19_TETTS Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis (PubMed:26551074). Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:26551074). The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis (PubMed:26551074).[1]
Publication Abstract from PubMed
Tetrahymena telomerase holoenzyme subunits p75, p45 and p19 form a subcomplex (7-4-1) peripheral to the catalytic core. We report structures of p45 and p19 and reveal them as the Stn1 and Ten1 subunits of the CST complex, which stimulates telomerase complementary-strand synthesis. 7-4-1 binds telomeric single-stranded DNA, and mutant p19 overexpression causes telomere 3'-overhang elongation. We propose that telomerase-tethered Tetrahymena CST coordinates telomere G-strand and C-strand synthesis.
The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex.,Wan B, Tang T, Upton H, Shuai J, Zhou Y, Li S, Chen J, Brunzelle JS, Zeng Z, Collins K, Wu J, Lei M Nat Struct Mol Biol. 2015 Nov 9. doi: 10.1038/nsmb.3126. PMID:26551074[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wan B, Tang T, Upton H, Shuai J, Zhou Y, Li S, Chen J, Brunzelle JS, Zeng Z, Collins K, Wu J, Lei M. The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex. Nat Struct Mol Biol. 2015 Nov 9. doi: 10.1038/nsmb.3126. PMID:26551074 doi:http://dx.doi.org/10.1038/nsmb.3126
- ↑ Wan B, Tang T, Upton H, Shuai J, Zhou Y, Li S, Chen J, Brunzelle JS, Zeng Z, Collins K, Wu J, Lei M. The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex. Nat Struct Mol Biol. 2015 Nov 9. doi: 10.1038/nsmb.3126. PMID:26551074 doi:http://dx.doi.org/10.1038/nsmb.3126
