Biochemical characterization of Balbiani ring premessenger RNP particles

Wurtz, Tilmann; Lönnroth, Anna; Daneholt, Bertil

doi:10.1007/bf00360431

Cited by 5 publications

(3 citation statements)

References 2 publications

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“…1). This was first suggested by the EM analysis of the Balbiani long mRNA (37 kb) in dipteran Chironomus tentans, which forms a dense 50 nm mRNP particle resulting in a ∼200-fold compaction of the mRNA relative to its linear length when it is fully extended and unstructured (Wurtz et al 1990a). Similarly, EM analysis of nuclear pretranslational mRNPs isolated from yeast shows these mRNPs are also compacted by at least ∼15fold (Batisse et al 2009).…”

Section: Nontranslating Mrnas Form Compacted Structuresmentioning

confidence: 89%

The landscape of eukaryotic mRNPs

Khong

Parker

2019

RNA

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The proper regulation of mRNA processing, localization, translation, and degradation occurs on mRNPs. However, the global principles of mRNP organization are poorly understood. We utilize the limited, but existing, information available to present a speculative synthesis of mRNP organization with the following key points. First, mRNPs form a compacted structure due to the inherent folding of RNA. Second, the ribosome is the principal mechanism by which mRNA regions are partially decompacted. Third, mRNPs are 50%-80% protein by weight, consistent with proteins modulating mRNP organization, but also suggesting the majority of mRNA sequences are not directly interacting with RNA-binding proteins. Finally, the ratio of mRNA-binding proteins to mRNAs is higher in the nucleus to allow effective RNA processing and limit the potential for nuclear RNA based aggregation. This synthesis of mRNP understanding provides a model for mRNP biogenesis, structure, and regulation with multiple implications.

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Section: Nontranslating Mrnas Form Compacted Structuresmentioning

confidence: 89%

The landscape of eukaryotic mRNPs

Khong

Parker

2019

RNA

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“…Already at release from the gene, these mRNPs are packaged and equipped with the majority of its associated proteins. BR1 and BR2 mRNPs have a protein content of about 60%, presumably corresponding to about 500 individual proteins [187]. Some proteins are likely to be present in multiple copies in a single mRNP.…”

Section: Mrnps In the Interchromatin Compartmentmentioning

confidence: 99%

Integration of mRNP formation and export

Björk

Wieslander

2017

Cell. Mol. Life Sci.

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Expression of protein-coding genes in eukaryotes relies on the coordinated action of many sophisticated molecular machineries. Transcription produces precursor mRNAs (pre-mRNAs) and the active gene provides an environment in which the pre-mRNAs are processed, folded, and assembled into RNA–protein (RNP) complexes. The dynamic pre-mRNPs incorporate the growing transcript, proteins, and the processing machineries, as well as the specific protein marks left after processing that are essential for export and the cytoplasmic fate of the mRNPs. After release from the gene, the mRNPs move by diffusion within the interchromatin compartment, making up pools of mRNPs. Here, splicing and polyadenylation can be completed and the mRNPs recruit the major export receptor NXF1. Export competent mRNPs interact with the nuclear pore complex, leading to export, concomitant with compositional and conformational changes of the mRNPs. We summarize the integrated nuclear processes involved in the formation and export of mRNPs.

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“… 26 , 27 Electron microscopy studies have shown that the ~35-kb Balbiani ring mRNA in C. tentans is compacted ~200-fold into a nuclear mRNP with a diameter of ~50 nm that changes shape during nuclear export. 28 , 29 S. cerevisiae mRNPs are similarly compacted into a heterogeneous set of particles with dimensions that correlate with transcript length. 30 , 31 In humans, data suggest that the exon junction complex (EJC) and serine and arginine-rich (SR) proteins cooperate to promote mRNA packaging 32 , 33 ; however, a lack of EJC components in S. cerevisiae indicates that other RBPs must fulfill this function.…”

Section: Introductionmentioning

confidence: 99%

Single-molecule quantitation of RNA-binding protein occupancy and stoichiometry defines a role for Yra1 (Aly/REF) in nuclear mRNP organization

Asada,

Dominguez,

Montpetit

2023

Cell Reports

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Biochemical characterization of Balbiani ring premessenger RNP particles

Cited by 5 publications

References 2 publications

The landscape of eukaryotic mRNPs

The landscape of eukaryotic mRNPs

Integration of mRNP formation and export

Single-molecule quantitation of RNA-binding protein occupancy and stoichiometry defines a role for Yra1 (Aly/REF) in nuclear mRNP organization

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