Tay1 Protein, a Novel Telomere Binding Factor from Yarrowia lipolytica
Year: 2010
Type: article
Abstract: Inspection of the complete genome of the yeast Yarrowia lipolytica for the presence of genes encoding homologues of known telomere-binding proteins surprisingly revealed no counterparts of typical yeast Myb domain-containing telomeric factors including Rap1 or Taz1. Instead, we identified a gene, YALIOD10923g, encoding a protein containing two Myb domains, exhibiting a high degree of similarity to the Myb domain of human telomeric proteins TRF1 and TRF2 and homologous to an essential fission yeast protein Mug152 whose expression is elevated during meiosis. The protein, which we named Tay1p (telomere-associated in Yarrowia lipolytica 1), was purified for biochemical studies. Using a model Y. lipolytica telomere, we demonstrate that the protein preferentially binds to Y. lipolytica telomeric tracts. Tay1p binds along the telomeric tract as dimers and larger oligomers, and it is able to remodel the telomeric DNA into both looped structures and synaptic complexes of two model telomere DNAs. The ability of Tay1p to induce dimerization of telomeres in vitro goes in line with its oligomeric nature, where each oligomer can employ several Myb domains to form intermolecular telomere clusters. We also provide experimental evidence that Tay1p may be associated with Y. lipolytica telomeres in vivo. Together with its homologues from Schizosaccharomyces pombe and several basidiomycetous fungi (Sánchez-Alonso, P., and Guzman, P. (2008) Fungal Genet. Biol. 45, S54-S62), Tay1p constitutes a novel family of putative telomeric factors whose analysis may be instrumental in understanding the function and evolution of double-stranded DNA telomeric proteins.
Source: Journal of Biological Chemistry
Language: English
Subfield: Physiology (medical)
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Funders: Howard Hughes Medical Institute, Univerzita Komenského v Bratislave, Slovak Academic Information Agency, Slovenská Akadémia Vied, University of Alberta, Institut National de la Recherche Agronomique, National Institutes of Health, National Institute of General Medical Sciences, Fogarty International Center, National Institute of Environmental Health Sciences
Awards: G2031575927, G244937450, G2774293502, DNA-Protein Interactions at the Replication Fork, The structure of the telomere as a sentinel of DNA damage., G5282781497, Nucleoprotein Structures at Telomeres and Sites of DNA Damage, G9000240336, Studies of Telomere Structure Using Yeast Model Systems
OpenAlex ID: W2015635728