ArticleProceedings of the National Academy of Sciences of the United States of America1995
A class of single-stranded telomeric DNA-binding proteins required for Rap1p localization in yeast nuclei.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Comparative Analysis of Normalization Methods for Network Propagation.Frontiers in genetics · 2019Article
- A three-state model for the regulation of telomerase by TERRA and hnRNPA1.Nucleic acids research · 2013Article
- Epistatic interaction between the K-homology domain protein HEK2 and SIR1 at HMR and telomeres in yeast.Journal of molecular biology · 2008Article
- The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein.The Biochemical journal · 2007Article
- Biogenesis of yeast telomerase depends on the importin mtr10.Molecular and cellular biology · 2002Article
- Yeast hnRNP K-like genes are involved in regulation of the telomeric position effect and telomere length.Molecular and cellular biology · 2002Article
- Telomere-binding and Stn1p-interacting activities are required for the essential function of Saccharomyces cerevisiae Cdc13p.Nucleic acids research · 2000Article
- Article
- The Est1 subunit of yeast telomerase binds the Tlc1 telomerase RNA.Molecular and cellular biology · 2000Article
- Gbp1p, a protein with RNA recognition motifs, binds single-stranded telomeric DNA and changes its binding specificity upon dimerization.Molecular and cellular biology · 1999Article
- Telomere length regulation and telomeric chromatin require the nonsense-mediated mRNA decay pathway.Molecular and cellular biology · 1998Article
- The C terminus of the major yeast telomere binding protein Rap1p enhances telomere formation.Molecular and cellular biology · 1998Article
- Functionally interacting telomerase RNAs in the yeast telomerase complex.Genes & development · 1997Article
- The clustering of telomeres and colocalization with Rap1, Sir3, and Sir4 proteins in wild-type Saccharomyces cerevisiae.The Journal of cell biology · 1996Article
- Cloning and expression of a gene encoding an integrin-like protein in Candida albicans.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified a class of proteins that bind single-stranded telomeric DNA and are required for the nuclear organization of telomeres and/or telomere-associated proteins. Rlf6p was identified by its sequence similarity to Gbp1p, a single-stranded telomeric DNA-binding protein from Chlamydomonas reinhardtii. Rlf6p and Gbp1p bind yeast single-stranded G-strand telomeric DNA. Both proteins include at least two RNA recognition motifs, which are found in many proteins that interact with single-stranded nucleic acids. Disruption of RLF6 alters the distribution of repressor/activator protein 1 (Rap1p), a telomere-associated protein. In wild-type yeast cells, Rap1p localizes to a small number of perinuclear spots, while in rlf6 cells Rap1p appears diffuse and nuclear. Interestingly, telomere position effect and telomere length control, which require RAP1, are unaffected by rlf6 mutations, demonstrating that Rap1p localization can be uncoupled from other Rap1p-dependent telomere functions. In addition, expression of Chlamydomonas GBP1 restores perinuclear, punctate Rap1p localization in rlf6 mutant cells. The functional complementation of a fungal gene by an algal gene suggests that Rlf6p and Gbp1p are members of a conserved class of single-stranded telomeric DNA-binding proteins that influence nuclear organization. Furthermore, it demonstrates that, despite their unusual codon bias, C. reinhardtii genes can be efficiently translated in Saccharomyces cerevisiae cells.
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