ArticleNucleic acids research2004
Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Alternative translation initiation by ribosomal leaky scanning produces multiple isoforms of the Pif1 helicase.Nucleic acids research · 2024Article
- A novel approach to analyze the association characteristics between post-spliced introns and their corresponding mRNA.Frontiers in genetics · 2023Article
- Adaptive expression responses in the Pol-gamma null strain of S. pombe depleted of mitochondrial genome.BMC genomics · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
DNA ligase I (Lig I) has key roles in chromosomal DNA replication and repair in the eukaryotic cell nucleus. In the budding yeast Saccharomyces cerevisiae the Lig I enzyme Cdc9p is also required for mitochondrial DNA replication and repair. In this report, dual nuclear-mitochondrial localization is demonstrated to be a property of the essential Lig I enzyme Cdc17 from the distantly related fission yeast Schizosaccharomyces pombe. Expression of nuclear and mitochondrial forms of Cdc17 from separate genes shows that, whereas expression of either protein alone is insufficient to restore viability to cells lacking endogenous Cdc17, co-expression restores full viability. In the nucleus, Lig I interacts with the sliding clamp proliferating cell nuclear antigen (PCNA) via a conserved PCNA interacting sequence motif known as a PIP box. Deletion of the PIP motif from the N-terminus of the nuclear form of Cdc17 fails to abolish Cdc17 function, indicating that PCNA binding by Cdc17 is not an absolute requirement for completion of S-phase.
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Registered trials
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