ArticleThe Journal of cell biology1995
Structural interaction between the nuclear pore complex and a specific translocating RNP particle.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed.
- Spatial Organization of Single mRNPs at Different Stages of the Gene Expression Pathway.Molecular cell · 2018Article
- Integration of mRNP formation and export.Cellular and molecular life sciences : CMLS · 2017Review
- Temporal and spatial regulation of mRNA export: Single particle RNA-imaging provides new tools and insights.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Intranuclear binding in space and time of exon junction complex and NXF1 to premRNPs/mRNPs in vivo.The Journal of cell biology · 2015Article
- An agent-based model for mRNA export through the nuclear pore complex.Molecular biology of the cell · 2014Article
- The Chironomus tentans genome sequence and the organization of the Balbiani ring genes.BMC genomics · 2014Article
- Review
- Nuclear export, enlightened.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Review
- Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex.Journal of cell science · 2010Article
- The Ct-RAE1 protein interacts with Balbiani ring RNP particles at the nuclear pore.RNA (New York, N.Y.) · 2000Article
- Nuclear import of plasmid DNA in digitonin-permeabilized cells requires both cytoplasmic factors and specific DNA sequences.The Journal of biological chemistry · 1999Article
- RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains.The Journal of cell biology · 1999Article
- Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export.The EMBO journal · 1998Article
- Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA.The EMBO journal · 1998Article
- mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export.The Journal of cell biology · 1996Article
- Jumping over the fence: RNA nuclear export revisited.Nucleus (Austin, Tex.)Article
- The dynamic pathway of nuclear RNA in eukaryotes.Nucleus (Austin, Tex.)Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transport of Balbiani ring (BR) premessenger RNP particles in the larval salivary gland cells of the dipteran Chironomus tentans can be followed using electron microscopy. A BR RNP particle consists of an RNP ribbon bent into a ringlike structure. Upon translocation through the nuclear pore complex (NPC), the ribbon is straightened and enters the central channel of the NPC with the 5' end of the transcript in the lead. The translocating ribbon is likely to interact with the central channel but, in addition, the remaining portion of the ribbon ring makes contact with the periphery of the NPC. To determine the nature of this latter interaction, we have now studied the connections between the RNP particle and the border of the NPC during different stages of translocation using electron microscope tomography. It was observed that the 3' terminal domain of the ribbon always touches the nuclear ring of the NPC, but the precise area of contact is variable. Sometimes also a region on the opposite side of the ribbon ring reaches the nuclear ring. The pattern of contacts could be correlated to the stage of translocation, and it was concluded that the particle-nuclear ring interactions reflect a rotation of the ribbon ring in front of the central channel, the rotation being secondary to the successive translocation of the ribbon through the channel. The particle's mode of interaction with the NPC suggests that the initial contact between the 5' end domain of the ribbon and the entrance to the central channel is probably crucial to accomplish the ordered translocation of the premessenger RNP particle through the NPC.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.