ArticleMolecular and cellular biology1995
ST-1, a 39-kilodalton protein in Trypanosoma brucei, exhibits a dual affinity for the duplex form of the 29-base-pair subtelomeric repeat and its C-rich strand.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 32 citations in OpenAlex.
- Probing the Potential Role of Non-B DNA Structures at Yeast Meiosis-Specific DNA Double-Strand Breaks.Biophysical journal · 2017Article
- Telomere components as potential therapeutic targets for treating microbial pathogen infections.Frontiers in oncology · 2012Article
- Trypanosome telomeres are protected by a homologue of mammalian TRF2.Molecular and cellular biology · 2005Article
- Telomere maintenance and length regulation in Trypanosoma brucei.The EMBO journal · 2000Article
- Identification of two human nuclear proteins that recognise the cytosine-rich strand of human telomeres in vitro.Nucleic acids research · 2000Article
- A single-stranded DNA-binding protein shared by telomeric repeats, the variant surface glycoprotein transcription promoter and the procyclin transcription terminator of Trypanosoma brucei.Nucleic acids research · 2000Article
- Characterisation of Leishmania telomeres reveals unusual telomeric repeats and conserved telomere-associated sequence.Nucleic acids research · 1998Article
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2 authors at 1 institution in 1 country.
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Abstract
In our attempt to identify telomere region-binding proteins in Trypanosoma brucei, we identified ST-1, a polypeptide with novel features. ST-1 was chromatographically purified from S-100 cell extracts and was renatured from a sodium dodecyl sulfate-protein gel as a 39-kDa polypeptide. It forms a specific complex with the trypanosome telomere repeats of TTAGGG, but more significantly, it shows a higher affinity for the 29-bp subtelomere repeats of T. brucei. These 29-mer boxes are a large tandem series of telomere-derived repeats which separate the simple telomere DNA from middle-repetitive telomere-associated sequences on many chromosomes. ST-1 is the first example of a protein binding within such large repetitive subtelomere elements in trypanosomes or other organisms. ST-1 is also novel in that it has a selective affinity for the C-rich strands of both the subtelomeric 29-mer and the telomere repeats, comparable to that for the duplex form of the respective repeats. All previously described telomere-binding proteins have affinity for only the duplex form or for the G-rich strand. This C-rich strand binding specificity of ST-1 may provide insight into this protein's mechanism of binding in vivo.
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