ArticleNucleic acids research1996
DNA-protein interactions at the telomeric repeats of Schizosaccharomyces pombe.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Fission yeast telosomes: non-canonical histone-containing chromatin structures dependent on shelterin and RNA.Nucleic acids research · 2018Article
- A Matter of Scale and Dimensions: Chromatin of Chromosome Landmarks in the Fungi.Microbiology spectrum · 2017Review
- Replication proteins influence the maintenance of telomere length and telomerase protein stability.Molecular and cellular biology · 2003Article
- Sequence-specific binding of Taz1p dimers to fission yeast telomeric DNA.Nucleic acids research · 2000Article
- Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation.Molecular and cellular biology · 1999Article
- Regulation of telomere length by checkpoint genes in Schizosaccharomyces pombe.Molecular biology of the cell · 1998Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gel retardation assays using a probe containing the repeat region of a Schizosaccharomyces pombe chromosomal telomere identified four specific DNA- protein complexes in S. pombe total protein extracts (I, I', IIa and IIb). The proteins responsible for these complexes bound to the telomeric repeat region irrespective of whether or not the repeats were in close proximity to the end of a DNA molecule, and none of them bound strongly to single-stranded DNA. The protein responsible for complex I (TeRF I) was separated from the activity responsible for complexes IIa and IIb (TeRF II) using heparin-Sepharose chromatography. Both factors were efficiently cross-competed by an oligonucleotide containing the 18 bp sequence 5'-GGTTACAGGTTACAGGTT-3', which corresponds to two complete telomeric repeat units. Mutation of the T residues at positions 4 and 11 in the oligonucleotide dramatically reduced binding by TeRF II, but had no affect on binding by TeRF I. The protein responsible for complex I' did not bind strongly to either the wild-type or mutant oligonucleotide.
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