ArticleThe Biochemical journal2007
The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Phenome-wide analyses identify an association between the parent-of-origin effects dependent methylome and the rate of aging in humans.Genome biology · 2023Article
- IMP4 Silencing Inhibits the Malignancy of Lung Adenocarcinoma via ERK Pathway.Journal of oncology · 2022Article
- Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis.Nucleic acids research · 2015Article
- Telomeric transcripts stimulate telomere recombination to suppress senescence in cells lacking telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A viable hypomorphic allele of the essential IMP3 gene reveals novel protein functions in Saccharomyces cerevisiae.PloS one · 2011Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Imp4p is a component of U3 snoRNP (small nucleolar ribonucleoprotein) involved in the maturation of 18S rRNA. We have shown that Imp4p interacts with Cdc13p, a single-stranded telomere-binding protein involved in telomere maintenance. To understand the role of Imp4p in telomeres, we purified recombinant Imp4p protein and tested its binding activity towards telomeric DNA using electrophoretic mobility-shift assays. Our results showed that Imp4p bound specifically to single-stranded telomeric DNA in vitro. The interaction of Imp4p to telomeres in vivo was also demonstrated by chromatin immunoprecipitation experiments. Significantly, the binding of Imp4p to telomeres was not limited to yeast proteins, since the hImp4 (human Imp4) also bound to vertebrate single-stranded telomeric DNA. Thus we conclude that Imp4p is a novel telomeric DNA-binding protein that, in addition to its role in rRNA processing, might participate in telomere function.
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