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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. Expand
Human Rad51 Protein Promotes ATP-Dependent Homologous Pairing and Strand Transfer Reactions In Vitro
The results establish hRad51 as a functional homolog of RecA, but indicate that the human protein and its bacterial counterpart differ in their ability to promote extensive strand transfer. Expand
Comparative Functional Genomics of the Fission Yeasts
Differences in gene content and regulation explain why, unlike the budding yeast of Saccharomycotina, fission yeasts cannot use ethanol as a primary carbon source and provide tools for investigation across the Schizosaccharomyces clade. Expand
DNA end-joining catalyzed by human cell-free extracts.
- P. Baumann, S. West
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 24 November 1998
Using cell-free extracts prepared from human lymphoblastoid cell lines, an in vitro system for end-joining has been developed andIntermolecular ligation was found to be accurate and to depend on DNA ligase IV/Xrcc4 and requires Ku70, Ku86, and DNA-PKcs, the three subunits of the DNA-activated protein kinase DNA- PK. Expand
Synergistic actions of Rad51 and Rad52 in recombination and DNA repair
Yeast Rad51 has been shown to interact with Rad52 protein, as does the human homologue, and it is shown that hRad52 stimulates homologous pairing by hRad51, indicating that Rad52 is involved in an early stage of Rad51-mediated recombination. Expand
Role of the human RAD51 protein in homologous recombination and double-stranded-break repair.
The isolation of yeast and human RecA homologues shows that homologous recombination and recombinational repair have been conserved throughout evolution and the goal is now to identify other factors involved in recombinational Repair and to define their roles in this essential process. Expand
A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends.
Biochemical fractionation and reconstitution revealed that telomere protection is mediated by a RAP1/TRF2 complex, providing evidence for a direct role for human RAP 1 in the protection of telomeric DNA from NHEJ. Expand
DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA
The 1.9-Å-resolution crystal structure of the amino-terminal DNA-binding domain of S. pombe Pot1p complexed with ssDNA explains the sequence specificity of binding: in the context of the Pot1 protein, DNA self-recognition involving base-stacking and unusual G–T base pairs compacts the DNA. Expand
Human RAP1 inhibits non‐homologous end joining at telomeres
- Jay F. Sarthy, Nancy S. Bae, Jonathan D. Scrafford, P. Baumann
- Biology, Medicine
- The EMBO journal
- 4 November 2009
It is shown that TRF2 inhibits NHEJ, in part, by recruiting human RAP1 to telomeres, and this work identifies hRAP1 as a mediator of genome stability. Expand
Human Pot1 (Protection of Telomeres) Protein: Cytolocalization, Gene Structure, and Alternative Splicing
Using indirect immunofluorescence, it is shown that epitope-tagged hPot1 localizes to telomeres in interphase nuclei of human cells, consistent with a direct role in telomere end protection. Expand