Orchestrating ribosomal RNA folding during ribosome assembly

Oborská-Oplová, Michaela; Gerhardy, Stefan; Panse, Vikram Govind

doi:10.1002/bies.202200066

Cited by 5 publications

(3 citation statements)

References 157 publications

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“…We speculate that such an environment could be conducive to snoRNA- and protein chaperone-mediated regulation of rRNA folding, as observed in previous studies. 69 , 70 Further, this kinetic and material-based model could explain how that process is spatiotemporally regulated during the modular steps of ribosome biogenesis. 26 Indeed, our physical picture suggests that the nucleolus will exhibit spatially dependent viscoelasticity, with the most peripheral regions of the GC, farthest from nascent transcriptional sites at the FC/DFC interface, likely exhibiting behavior closest to that of a purely liquid condensate.…”

Section: Discussionmentioning

confidence: 97%

Viscoelasticity and advective flow of RNA underlies nucleolar form and function

Riback,

Eeftens,

Lee

et al. 2023

Molecular Cell

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Section: Discussionmentioning

confidence: 97%

Viscoelasticity and advective flow of RNA underlies nucleolar form and function

Riback,

Eeftens,

Lee

et al. 2023

Molecular Cell

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“…Both the binding of snoRNAs to the pre‐rRNA and the resulting nucleotide modifications play important roles in pre‐rRNA folding (see recent reviews Mitterer & Pertschy, 2022 ; Oborská‐Oplová et al , 2022 ). Many snoRNA binding sites are found in pre‐rRNA regions that fold late during nucleolar assembly steps.…”

Section: Pre‐rrna Modificationmentioning

confidence: 99%

Ribosome biogenesis factors—from names to functions

et al. 2023

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The assembly of ribosomal subunits is a highly orchestrated process that involves a huge cohort of accessory factors. Most eukaryotic ribosome biogenesis factors were first identified by genetic screens and proteomic approaches of pre‐ribosomal particles in Saccharomyces cerevisiae. Later, research on human ribosome synthesis not only demonstrated that the requirement for many of these factors is conserved in evolution, but also revealed the involvement of additional players, reflecting a more complex assembly pathway in mammalian cells. Yet, it remained a challenge for the field to assign a function to many of the identified factors and to reveal their molecular mode of action. Over the past decade, structural, biochemical, and cellular studies have largely filled this gap in knowledge and led to a detailed understanding of the molecular role that many of the players have during the stepwise process of ribosome maturation. Such detailed knowledge of the function of ribosome biogenesis factors will be key to further understand and better treat diseases linked to disturbed ribosome assembly, including ribosomopathies, as well as different types of cancer.

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“…Ribosome assembly has been studied over many decades and, despite its complexity and technical limitations, various aspects of the process are well understood. There are several reviews that provide detailed overviews of various aspects of the assembly process [1,20,21,[24][25][26][27][28][29][30]. Here, we aim to provide a methodological perspective on studying ribosome assembly and the assembly of other RNPs, such as the spliceosome, various mRNPs, and large non-coding RNPs.…”

Section: Introductionmentioning

confidence: 99%

Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein–RNA Complex Assembly

Gor

Duss

2023

Biomolecules

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Ribosome assembly is one of the most fundamental processes of gene expression and has served as a playground for investigating the molecular mechanisms of how protein–RNA complexes (RNPs) assemble. A bacterial ribosome is composed of around 50 ribosomal proteins, several of which are co-transcriptionally assembled on a ~4500-nucleotide-long pre-rRNA transcript that is further processed and modified during transcription, the entire process taking around 2 min in vivo and being assisted by dozens of assembly factors. How this complex molecular process works so efficiently to produce an active ribosome has been investigated over decades, resulting in the development of a plethora of novel approaches that can also be used to study the assembly of other RNPs in prokaryotes and eukaryotes. Here, we review biochemical, structural, and biophysical methods that have been developed and integrated to provide a detailed and quantitative understanding of the complex and intricate molecular process of bacterial ribosome assembly. We also discuss emerging, cutting-edge approaches that could be used in the future to study how transcription, rRNA processing, cellular factors, and the native cellular environment shape ribosome assembly and RNP assembly at large.

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Orchestrating ribosomal RNA folding during ribosome assembly

Cited by 5 publications

References 157 publications

Viscoelasticity and advective flow of RNA underlies nucleolar form and function

Viscoelasticity and advective flow of RNA underlies nucleolar form and function

Ribosome biogenesis factors—from names to functions

Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein–RNA Complex Assembly

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