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Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
It now appears that the protein that caps the ends of chromosomes is widely dispersed throughout the eukaryotic kingdom.
The POT1–TPP1 telomere complex is a telomerase processivity factor
The crystal structure of a domain of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the β-subunit of the telomere end-binding protein of a ciliated protozoan, suggesting that TPP1 is the missing β- subunit of human POT1 protein.
Reverse transcriptase motifs in the catalytic subunit of telomerase.
The reverse transcriptase protein fold, previously known to be involved in retroviral replication and retrotransposition, is essential for normal chromosome telomere replication in diverse eukaryotes.
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
The crystal structure of the N-terminal half of human POT1 (hPOT1) protein bound to a telomeric single-stranded DNA (ssDNA) decamer, TTAGGGTTAG, is reported, providing an atomic-resolution model for chromosome end-capping.
Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing
The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.
Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of tetrahymena
Self-splicing of group I introns.
- T. Cech
- Chemistry, BiologyAnnual Review of Biochemistry
The Tetrahymena INTRON is described as a “spatially aggregating force” that “brings together the determinants of infectious disease and infectious disease in a synergistic manner”.
Regulation of telomere length and function by a Myb-domain protein in fission yeast
A genetic screen is used to identify a telomere protein in fission yeast, Tazlp (telomere-associated in Schizosaccharomyces pombe), that shares homology to the Myb proto-oncogene DNA-binding domain with hTRF, and may protect against activation of telomerase-independent pathways of telomeres elongation.
Promiscuous RNA binding by Polycomb Repressive Complex 2
- C. Davidovich, Leon Zheng, K. Goodrich, T. Cech
- BiologyNature Structural &Molecular Biology
- 23 September 2013
These findings support a model in which PRC2's promiscuous binding to RNA transcripts allows it to scan for target genes that have escaped repression, thus leading to maintenance of the repressed state.
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity
Seven separation-of-function mutants of human TPP1 are identified that retain full telomere-capping function in vitro and in vivo, yet are defective in binding human telomerase.