ArticleDNA and cell biology2011
The karyopherin Kap95 and the C-termini of Rfa1, Rfa2, and Rfa3 are necessary for efficient nuclear import of functional RPA complex proteins in Saccharomyces cerevisiae.
Article in DNA and cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Functional genomic analysis of genes important for Candida albicans fitness in diverse environmental conditions.Cell reports · 2024Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Rtt105 promotes high-fidelity DNA replication and repair by regulating the single-stranded DNA-binding factor RPA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Microscopy analysis of the smallest subunit of the RPA complex, Rfa3p, prompts consideration of how RPA subunits gather at single-stranded DNA sites.microPublication biology · 2021Article
- Chaperoning RPA during DNA metabolism.Current genetics · 2019Review
- A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.Nature communications · 2018Article
- Rtt105 functions as a chaperone for replication protein A to preserve genome stability.The EMBO journal · 2018Article
- DNA resection proteins Sgs1 and Exo1 are required for G1 checkpoint activation in budding yeast.DNA repair · 2013Article
- Yeast importin-β is required for nuclear import of the Mig2 repressor.BMC cell biology · 2012Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear protein import in eukaryotic cells is mediated by karyopherin proteins, which bind to specific nuclear localization signals on substrate proteins and transport them across the nuclear envelope and into the nucleus. Replication protein A (RPA) is a nuclear protein comprised of three subunits (termed Rfa1, Rfa2, and Rfa3 in Saccharomyces cerevisiae) that binds single-stranded DNA and is essential for DNA replication, recombination, and repair. RPA associates with two different karyopherins in yeast, Kap95, and Msn5/Kap142. However, it is unclear which of these karyopherins is responsible for RPA nuclear import. We have generated GFP fusion proteins with each of the RPA subunits and demonstrate that these Rfa-GFP chimeras are functional in yeast cells. The intracellular localization of the RPA proteins in live cells is similar in wild-type and msn5Δ deletion strains but becomes primarily cytoplasmic in cells lacking functional Kap95. Truncating the C-terminus of any of the RPA subunits results in mislocalization of the proteins to the cytoplasm and a loss of protein-protein interactions between the subunits. Our data indicate that Kap95 is likely the primary karyopherin responsible for RPA nuclear import in yeast and that the C-terminal regions of Rfa1, Rfa2, and Rfa3 are essential for efficient nucleocytoplasmic transport of each RPA subunit.
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