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Journal articles on the topic 'Ribosomal biogenesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Moraleva, Anastasia A., Alexander S. Deryabin, Yury P. Rubtsov, Maria P. Rubtsova, and Olga A. Dontsova. "Eukaryotic Ribosome Biogenesis: The 40S Subunit." Acta Naturae 14, no. 1 (2022): 14–30. http://dx.doi.org/10.32607/actanaturae.11540.

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The formation of eukaryotic ribosomes is a sequential process of ribosomal precursors maturation in the nucleolus, nucleoplasm, and cytoplasm. Hundreds of ribosomal biogenesis factors ensure the accurate processing and formation of the ribosomal RNAs tertiary structure, and they interact with ribosomal proteins. Most of what we know about the ribosome assembly has been derived from yeast cell studies, and the mechanisms of ribosome biogenesis in eukaryotes are considered quite conservative. Although the main stages of ribosome biogenesis are similar across different groups of eukaryotes, this

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2

Moraleva, Anastasia A., Alexander S. Deryabin, Yury P. Rubtsov, Maria P. Rubtsova, and Olga A. Dontsova. "Eukaryotic Ribosome Biogenesis: The 60S Subunit." Acta Naturae 14, no. 2 (2022): 39–49. http://dx.doi.org/10.32607/actanaturae.11541.

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Ribosome biogenesis is consecutive coordinated maturation of ribosomal precursors in the nucleolus, nucleoplasm, and cytoplasm. The formation of mature ribosomal subunits involves hundreds of ribosomal biogenesis factors that ensure ribosomal RNA processing, tertiary structure, and interaction with ribosomal proteins. Although the main features and stages of ribosome biogenesis are conservative among different groups of eukaryotes, this process in human cells has become more complicated due to the larger size of the ribosomes and pre-ribosomes and intricate regulatory pathways affecting their

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3

Sulima, Sergey, Kim Kampen, and Kim De Keersmaecker. "Cancer Biogenesis in Ribosomopathies." Cells 8, no. 3 (2019): 229. http://dx.doi.org/10.3390/cells8030229.

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Ribosomopathies are congenital diseases with defects in ribosome assembly and are characterized by elevated cancer risks. Additionally, somatic mutations in ribosomal proteins have recently been linked to a variety of cancers. Despite a clear correlation between ribosome defects and cancer, the molecular mechanisms by which these defects promote tumorigenesis are unclear. In this review, we focus on the emerging mechanisms that link ribosomal defects in ribosomopathies to cancer progression. This includes functional “onco-specialization” of mutant ribosomes, extra-ribosomal consequences of mut

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Pecoraro, Annalisa, Martina Pagano, Giulia Russo, and Annapina Russo. "Ribosome Biogenesis and Cancer: Overview on Ribosomal Proteins." International Journal of Molecular Sciences 22, no. 11 (2021): 5496. http://dx.doi.org/10.3390/ijms22115496.

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Cytosolic ribosomes (cytoribosomes) are macromolecular ribonucleoprotein complexes that are assembled from ribosomal RNA and ribosomal proteins, which are essential for protein biosynthesis. Mitochondrial ribosomes (mitoribosomes) perform translation of the proteins essential for the oxidative phosphorylation system. The biogenesis of cytoribosomes and mitoribosomes includes ribosomal RNA processing, modification and binding to ribosomal proteins and is assisted by numerous biogenesis factors. This is a major energy-consuming process in the cell and, therefore, is highly coordinated and sensit

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5

Konikkat, Salini, and John L. Woolford,. "Principles of 60S ribosomal subunit assembly emerging from recent studies in yeast." Biochemical Journal 474, no. 2 (2017): 195–214. http://dx.doi.org/10.1042/bcj20160516.

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Ribosome biogenesis requires the intertwined processes of folding, modification, and processing of ribosomal RNA, together with binding of ribosomal proteins. In eukaryotic cells, ribosome assembly begins in the nucleolus, continues in the nucleoplasm, and is not completed until after nascent particles are exported to the cytoplasm. The efficiency and fidelity of ribosome biogenesis are facilitated by >200 assembly factors and ∼76 different small nucleolar RNAs. The pathway is driven forward by numerous remodeling events to rearrange the ribonucleoprotein architecture of pre-ribosomes. Here

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6

Sleiman, Sophie, and Francois Dragon. "Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10." Cells 8, no. 9 (2019): 1035. http://dx.doi.org/10.3390/cells8091035.

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Ribosome biogenesis is one of the most energy demanding processes in the cell. In eukaryotes, the main steps of this process occur in the nucleolus and include pre-ribosomal RNA (pre-rRNA) processing, post-transcriptional modifications, and assembly of many non-ribosomal factors and ribosomal proteins in order to form mature and functional ribosomes. In yeast and humans, the nucleolar RNA acetyltransferase Kre33/NAT10 participates in different maturation events, such as acetylation and processing of 18S rRNA, and assembly of the 40S ribosomal subunit. Here, we review the structural and functio

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7

Lavdovskaia, Elena, Kärt Denks, Franziska Nadler, et al. "Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes." Nucleic Acids Research 48, no. 22 (2020): 12929–42. http://dx.doi.org/10.1093/nar/gkaa1132.

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Abstract Translation and ribosome biogenesis in mitochondria require auxiliary factors that ensure rapid and accurate synthesis of mitochondrial proteins. Defects in translation are associated with oxidative phosphorylation deficiency and cause severe human diseases, but the exact roles of mitochondrial translation-associated factors are not known. Here we identify the functions of GTPBP6, a homolog of the bacterial ribosome-recycling factor HflX, in human mitochondria. Similarly to HflX, GTPBP6 facilitates the dissociation of ribosomes in vitro and in vivo. In contrast to HflX, GTPBP6 is also

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8

Phan, Tamara, Fatima Khalid, and Sebastian Iben. "Nucleolar and Ribosomal Dysfunction—A Common Pathomechanism in Childhood Progerias?" Cells 8, no. 6 (2019): 534. http://dx.doi.org/10.3390/cells8060534.

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The nucleolus organizes around the sites of transcription by RNA polymerase I (RNA Pol I). rDNA transcription by this enzyme is the key step of ribosome biogenesis and most of the assembly and maturation processes of the ribosome occur co-transcriptionally. Therefore, disturbances in rRNA transcription and processing translate to ribosomal malfunction. Nucleolar malfunction has recently been described in the classical progeria of childhood, Hutchinson–Gilford syndrome (HGPS), which is characterized by severe signs of premature aging, including atherosclerosis, alopecia, and osteoporosis. A der

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9

Slimane, Sophie Nait, Virginie Marcel, Tanguy Fenouil, et al. "Ribosome Biogenesis Alterations in Colorectal Cancer." Cells 9, no. 11 (2020): 2361. http://dx.doi.org/10.3390/cells9112361.

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Many studies have focused on understanding the regulation and functions of aberrant protein synthesis in colorectal cancer (CRC), leaving the ribosome, its main effector, relatively underappreciated in CRC. The production of functional ribosomes is initiated in the nucleolus, requires coordinated ribosomal RNA (rRNA) processing and ribosomal protein (RP) assembly, and is frequently hyperactivated to support the needs in protein synthesis essential to withstand unremitting cancer cell growth. This elevated ribosome production in cancer cells includes a strong alteration of ribosome biogenesis h

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10

Larson, D. E., P. Zahradka, and B. H. Sells. "Control points in eucaryotic ribosome biogenesis." Biochemistry and Cell Biology 69, no. 1 (1991): 5–22. http://dx.doi.org/10.1139/o91-002.

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Ribosome biogenesis in eucaryotic cells involves the coordinated synthesis of four rRNA species, transcribed by RNA polymerase I (18S, 28S, 5.8S) and RNA polymerase III (5S), and approximately 80 ribosomal proteins translated from mRNAs synthesized by RNA polymerase II. Assembly of the ribosomal subunits in the nucleolus, the site of 45S rRNA precursor gene transcription, requires the movement of 5S rRNA and ribosomal proteins from the nucleoplasm and cytoplasm, respectively, to this structure. To integrate these events and ensure the balanced production of individual ribosomal components, dif

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11

Roychowdhury, Amlan, Clément Joret, Gabrielle Bourgeois, Valérie Heurgué-Hamard, Denis L. J. Lafontaine, and Marc Graille. "The DEAH-box RNA helicase Dhr1 contains a remarkable carboxyl terminal domain essential for small ribosomal subunit biogenesis." Nucleic Acids Research 47, no. 14 (2019): 7548–63. http://dx.doi.org/10.1093/nar/gkz529.

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Abstract Ribosome biogenesis is an essential process in all living cells, which entails countless highly sequential and dynamic structural reorganization events. These include formation of dozens RNA helices through Watson-Crick base-pairing within ribosomal RNAs (rRNAs) and between rRNAs and small nucleolar RNAs (snoRNAs), transient association of hundreds of proteinaceous assembly factors to nascent precursor (pre-)ribosomes, and stable assembly of ribosomal proteins. Unsurprisingly, the largest group of ribosome assembly factors are energy-consuming proteins (NTPases) including 25 RNA helic

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12

Albanèse, Véronique, Stefanie Reissmann, and Judith Frydman. "A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis." Journal of Cell Biology 189, no. 1 (2010): 69–81. http://dx.doi.org/10.1083/jcb.201001054.

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Molecular chaperones assist cellular protein folding as well as oligomeric complex assembly. In eukaryotic cells, several chaperones termed chaperones linked to protein synthesis (CLIPS) are transcriptionally and physically linked to ribosomes and are implicated in protein biosynthesis. In this study, we show that a CLIPS network comprising two ribosome-anchored J-proteins, Jjj1 and Zuo1, function together with their partner Hsp70 proteins to mediate the biogenesis of ribosomes themselves. Jjj1 and Zuo1 have overlapping but distinct functions in this complex process involving the coordinated a

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13

Datta, Kaustuv, Jennifer L. Fuentes, and Janine R. Maddock. "The Yeast GTPase Mtg2p Is Required for Mitochondrial Translation and Partially Suppresses an rRNA Methyltransferase Mutant,mrm2." Molecular Biology of the Cell 16, no. 2 (2005): 954–63. http://dx.doi.org/10.1091/mbc.e04-07-0622.

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The assembly of ribosomes involves the coordinated processing and modification of rRNAs with the temporal association of ribosomal proteins. This process is regulated by assembly factors such as helicases, modifying enzymes, and GTPases. In contrast to the assembly of cytoplasmic ribosomes, there is a paucity of information concerning the role of assembly proteins in the biogenesis of mitochondrial ribosomes. In this study, we demonstrate that the Saccharomyces cerevisiae GTPase Mtg2p (Yhr168wp) is essential for mitochondrial ribosome function. Cells lacking MTG2 lose their mitochondrial DNA,

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14

Collins, Jason C., Homa Ghalei, Joanne R. Doherty, Haina Huang, Rebecca N. Culver, and Katrin Karbstein. "Ribosome biogenesis factor Ltv1 chaperones the assembly of the small subunit head." Journal of Cell Biology 217, no. 12 (2018): 4141–54. http://dx.doi.org/10.1083/jcb.201804163.

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The correct assembly of ribosomes from ribosomal RNAs (rRNAs) and ribosomal proteins (RPs) is critical, as indicated by the diseases caused by RP haploinsufficiency and loss of RP stoichiometry in cancer cells. Nevertheless, how assembly of each RP is ensured remains poorly understood. We use yeast genetics, biochemistry, and structure probing to show that the assembly factor Ltv1 facilitates the incorporation of Rps3, Rps10, and Asc1/RACK1 into the small ribosomal subunit head. Ribosomes from Ltv1-deficient yeast have substoichiometric amounts of Rps10 and Asc1 and show defects in translation

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15

Destefanis, Francesca, Valeria Manara, and Paola Bellosta. "Myc as a Regulator of Ribosome Biogenesis and Cell Competition: A Link to Cancer." International Journal of Molecular Sciences 21, no. 11 (2020): 4037. http://dx.doi.org/10.3390/ijms21114037.

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The biogenesis of ribosomes is a finely regulated multistep process linked to cell proliferation and growth—processes which require a high rate of protein synthesis. One of the master regulators of ribosome biogenesis is Myc, a well-known proto-oncogene that has an important role in ribosomal function and in the regulation of protein synthesis. The relationship between Myc and the ribosomes was first highlighted in Drosophila, where Myc’s role in controlling Pol-I, II and III was evidenced by both microarrays data, and by the ability of Myc to control growth (mass), and cellular and animal siz

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16

Temaj, Gazmend, Silvia Chichiarelli, Margherita Eufemi, et al. "Ribosome-Directed Therapies in Cancer." Biomedicines 10, no. 9 (2022): 2088. http://dx.doi.org/10.3390/biomedicines10092088.

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The human ribosomes are the cellular machines that participate in protein synthesis, which is deeply affected during cancer transformation by different oncoproteins and is shown to provide cancer cell proliferation and therefore biomass. Cancer diseases are associated with an increase in ribosome biogenesis and mutation of ribosomal proteins. The ribosome represents an attractive anti-cancer therapy target and several strategies are used to identify specific drugs. Here we review the role of different drugs that may decrease ribosome biogenesis and cancer cell proliferation.

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17

Levy, Michael, Reuven Falkovich, Shirley S. Daube, and Roy H. Bar-Ziv. "Autonomous synthesis and assembly of a ribosomal subunit on a chip." Science Advances 6, no. 16 (2020): eaaz6020. http://dx.doi.org/10.1126/sciadv.aaz6020.

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Ribosome biogenesis is an efficient and complex assembly process that has not been reconstructed outside a living cell so far, yet is the most critical step for establishing a self-replicating artificial cell. We recreated the biogenesis of Escherichia coli’s small ribosomal subunit by synthesizing and capturing all its ribosomal proteins and RNA on a chip. Surface confinement provided favorable conditions for autonomous stepwise assembly of new subunits, spatially segregated from original intact ribosomes. Our real-time fluorescence measurements revealed hierarchal assembly, cooperative inter

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18

Lu, Yiwei, Shizhuo Wang, and Yisheng Jiao. "The Effects of Deregulated Ribosomal Biogenesis in Cancer." Biomolecules 13, no. 11 (2023): 1593. http://dx.doi.org/10.3390/biom13111593.

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Ribosomes are macromolecular ribonucleoprotein complexes assembled from RNA and proteins. Functional ribosomes arise from the nucleolus, require ribosomal RNA processing and the coordinated assembly of ribosomal proteins (RPs), and are frequently hyperactivated to support the requirement for protein synthesis during the self-biosynthetic and metabolic activities of cancer cells. Studies have provided relevant information on targeted anticancer molecules involved in ribosome biogenesis (RiBi), as increased RiBi is characteristic of many types of cancer. The association between unlimited cell pr

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19

Harold, Cecelia M., Amber F. Buhagiar, Yan Cheng, and Susan J. Baserga. "Ribosomal RNA Transcription Regulation in Breast Cancer." Genes 12, no. 4 (2021): 502. http://dx.doi.org/10.3390/genes12040502.

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Ribosome biogenesis is a complex process that is responsible for the formation of ribosomes and ultimately global protein synthesis. The first step in this process is the synthesis of the ribosomal RNA in the nucleolus, transcribed by RNA Polymerase I. Historically, abnormal nucleolar structure is indicative of poor cancer prognoses. In recent years, it has been shown that ribosome biogenesis, and rDNA transcription in particular, is dysregulated in cancer cells. Coupled with advancements in screening technology that allowed for the discovery of novel drugs targeting RNA Polymerase I, this tra

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20

Shayan, Ramtin, Dana Rinaldi, Natacha Larburu, et al. "Good Vibrations: Structural Remodeling of Maturing Yeast Pre-40S Ribosomal Particles Followed by Cryo-Electron Microscopy." Molecules 25, no. 5 (2020): 1125. http://dx.doi.org/10.3390/molecules25051125.

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Assembly of eukaryotic ribosomal subunits is a very complex and sequential process that starts in the nucleolus and finishes in the cytoplasm with the formation of functional ribosomes. Over the past few years, characterization of the many molecular events underlying eukaryotic ribosome biogenesis has been drastically improved by the “resolution revolution” of cryo-electron microscopy (cryo-EM). However, if very early maturation events have been well characterized for both yeast ribosomal subunits, little is known regarding the final maturation steps occurring to the small (40S) ribosomal subu

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21

Sondalle, Samuel B., Simonne Longerich, Lisa M. Ogawa, Patrick Sung, and Susan J. Baserga. "Fanconi anemia protein FANCI functions in ribosome biogenesis." Proceedings of the National Academy of Sciences 116, no. 7 (2019): 2561–70. http://dx.doi.org/10.1073/pnas.1811557116.

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Fanconi anemia (FA) is a disease of DNA repair characterized by bone marrow failure and a reduced ability to remove DNA interstrand cross-links. Here, we provide evidence that the FA protein FANCI also functions in ribosome biogenesis, the process of making ribosomes that initiates in the nucleolus. We show that FANCI localizes to the nucleolus and is functionally and physically tied to the transcription of pre-ribosomal RNA (pre-rRNA) and to large ribosomal subunit (LSU) pre-rRNA processing independent of FANCD2. While FANCI is known to be monoubiquitinated when activated for DNA repair, we f

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Pollutri, Daniela, and Marianna Penzo. "Ribosomal Protein L10: From Function to Dysfunction." Cells 9, no. 11 (2020): 2503. http://dx.doi.org/10.3390/cells9112503.

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Eukaryotic cytoplasmic ribosomes are highly structured macromolecular complexes made up of four different ribosomal RNAs (rRNAs) and 80 ribosomal proteins (RPs), which play a central role in the decoding of genetic code for the synthesis of new proteins. Over the past 25 years, studies on yeast and human models have made it possible to identify RPL10 (ribosomal protein L10 gene), which is a constituent of the large subunit of the ribosome, as an important player in the final stages of ribosome biogenesis and in ribosome function. Here, we reviewed the literature to give an overview of the role

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Baßler, Jochen, and Ed Hurt. "Eukaryotic Ribosome Assembly." Annual Review of Biochemistry 88, no. 1 (2019): 281–306. http://dx.doi.org/10.1146/annurev-biochem-013118-110817.

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Ribosomes, which synthesize the proteins of a cell, comprise ribosomal RNA and ribosomal proteins, which coassemble hierarchically during a process termed ribosome biogenesis. Historically, biochemical and molecular biology approaches have revealed how preribosomal particles form and mature in consecutive steps, starting in the nucleolus and terminating after nuclear export into the cytoplasm. However, only recently, due to the revolution in cryo–electron microscopy, could pseudoatomic structures of different preribosomal particles be obtained. Together with in vitro maturation assays, these f

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24

Woellhaf, Michael W., Katja G. Hansen, Christoph Garth, and Johannes M. Herrmann. "Import of ribosomal proteins into yeast mitochondria." Biochemistry and Cell Biology 92, no. 6 (2014): 489–98. http://dx.doi.org/10.1139/bcb-2014-0029.

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Mitochondrial ribosomes of baker’s yeast contain at least 78 protein subunits. All but one of these proteins are nuclear-encoded, synthesized on cytosolic ribosomes, and imported into the matrix for biogenesis. The import of matrix proteins typically relies on N-terminal mitochondrial targeting sequences that form positively charged amphipathic helices. Interestingly, the N-terminal regions of many ribosomal proteins do not closely match the characteristics of matrix targeting sequences, suggesting that the import processes of these proteins might deviate to some extent from the general import

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Ojha, Sandeep, Sulochan Malla, and Shawn M. Lyons. "snoRNPs: Functions in Ribosome Biogenesis." Biomolecules 10, no. 5 (2020): 783. http://dx.doi.org/10.3390/biom10050783.

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Ribosomes are perhaps the most critical macromolecular machine as they are tasked with carrying out protein synthesis in cells. They are incredibly complex structures composed of protein components and heavily chemically modified RNAs. The task of assembling mature ribosomes from their component parts consumes a massive amount of energy and requires greater than 200 assembly factors. Among the most critical of these are small nucleolar ribonucleoproteins (snoRNPs). These are small RNAs complexed with diverse sets of proteins. As suggested by their name, they localize to the nucleolus, the site

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26

Jovanovic, Bogdan, Lisa Schubert, Fabian Poetz, and Georg Stoecklin. "Tagging of RPS9 as a tool for ribosome purification and identification of ribosome-associated proteins." Archives of Biological Sciences, no. 00 (2020): 57. http://dx.doi.org/10.2298/abs20120557j.

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Ribosomes, the catalytic machinery required for protein synthesis, are comprised of 4 ribosomal RNAs and about 80 ribosomal proteins in mammals. Ribosomes further interact with numerous associated factors that regulate their biogenesis and function. As mutations of ribosomal proteins and ribosome associated proteins cause many diseases, it is important to develop tools by which ribosomes can be purified efficiently and with high specificity. Here, we designed a method to purify ribosomes from human cell lines by C-terminally tagging human RPS9, a protein of the small ribosomal subunit. The tag

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27

Temaj, Gazmend, Rifat Hadziselimovic, Hilada Nefic, and Nexhibe Nuhii. "Ribosome biogenesis and ribosome therapy in cancer cells." Research Results in Pharmacology 8, no. (4) (2022): 15–24. https://doi.org/10.3897/rrpharmacology.8.81706.

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Introduction: The process of protein synthesis is a vital process for all kingdoms of life. The ribosome is a ribonucleoprotein complex that reads the genetic code, from messenger RNA (mRNA) to produce proteins and to tightly regulate and ensure cells growth. The fact that numerous diseases are caused by defect during the ribosome biogenesis is important to understand this pathway. Materials and methods: We have analyzed the literature for ribosome biogenesis and its links with different diseases which have been found. Results and discussion: We have discussed the key aspect of human ribosome

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28

Kazibwe, Zakayo, Ang-Yu Liu, Gustavo C. MacIntosh, and Diane C. Bassham. "The Ins and Outs of Autophagic Ribosome Turnover." Cells 8, no. 12 (2019): 1603. http://dx.doi.org/10.3390/cells8121603.

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Ribosomes are essential for protein synthesis in all organisms and their biogenesis and number are tightly controlled to maintain homeostasis in changing environmental conditions. While ribosome assembly and quality control mechanisms have been extensively studied, our understanding of ribosome degradation is limited. In yeast or animal cells, ribosomes are degraded after transfer into the vacuole or lysosome by ribophagy or nonselective autophagy, and ribosomal RNA can also be transferred directly across the lysosomal membrane by RNautophagy. In plants, ribosomal RNA is degraded by the vacuol

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Sugahara, Sho, Kana Unuma, Shuheng Wen, Takeshi Funakoshi, Toshihiko Aki, and Koichi Uemura. "Dissociation of mitochondrial and ribosomal biogenesis during thallium administration in rat kidney." PLOS ONE 19, no. 12 (2024): e0311884. https://doi.org/10.1371/journal.pone.0311884.

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Thallium (Tl) is a heavy metal with toxicity comparative to other heavy metals such as As, Cd, and Hg. Nevertheless, fewer studies have been reported concerning the molecular mechanism of Tl toxicity as compared to other heavy metals. To obtain insight into Tl toxicity in the kidney, rats were intraperitoneally administered Tl2SO4 (30 mg/kg), and the kidneys were removed 2 or 5 days later to examine the effects of Tl. Transcriptome analysis using DNA microarray of the rat kidney 2 and 5 days after Tl administration showed that cytoplasmic ribosomal proteins are the most upregulated category; m

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30

Temaj, Gazmend, Rifat Hadziselimovic, Hilada Nefic, and Nexhibe Nuhii. "Ribosome biogenesis and ribosome therapy in cancer cells." Research Results in Pharmacology 8, no. 4 (2022): 15–24. http://dx.doi.org/10.3897/rrpharmacology.8.81706.

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Introduction: The process of protein synthesis is a vital process for all kingdoms of life. The ribosome is a ribonucleoprotein complex that reads the genetic code, from messenger RNA (mRNA) to produce proteins and to tightly regulate and ensure cells growth. The fact that numerous diseases are caused by defect during the ribosome biogenesis is important to understand this pathway. Materials and methods: We have analyzed the literature for ribosome biogenesis and its links with different diseases which have been found. Results and discussion: We have discussed the key aspect of human ribosome

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Koplin, Ansgar, Steffen Preissler, Yulia Ilina, et al. "A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes." Journal of Cell Biology 189, no. 1 (2010): 57–68. http://dx.doi.org/10.1083/jcb.200910074.

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The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide–associated complex (NAC), another ribosome-tethered system, is functionally connected to SSB–RAC and the cytosolic Hsp70 network. Simultaneous deletions of genes encoding NAC and SSB caused conditional loss of cell viability under protein-folding stress conditions. Furthermore, NAC mutations revealed genetic interaction with a deletion of Sse1, a nucleotide exchange factor regul

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Choi, Ilyeong, Young Jeon, Youngki Yoo, Hyun-Soo Cho, and Hyun-Sook Pai. "The in vivo functions of ARPF2 and ARRS1 in ribosomal RNA processing and ribosome biogenesis in Arabidopsis." Journal of Experimental Botany 71, no. 9 (2020): 2596–611. http://dx.doi.org/10.1093/jxb/eraa019.

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Abstract Yeast Rpf2 plays a critical role in the incorporation of 5S rRNA into pre-ribosomes by forming a binary complex with Rrs1. The protein characteristics and overexpression phenotypes of Arabidopsis Ribosome Production Factor 2 (ARPF2) and Arabidopsis Regulator of Ribosome Synthesis 1 (ARRS1) have been previously studied. Here, we analyze loss-of-function phenotypes of ARPF2 and ARRS1 using virus-induced gene silencing to determine their functions in pre-rRNA processing and ribosome biogenesis. ARPF2 silencing in Arabidopsis led to pleiotropic developmental defects. RNA gel blot analysis

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Pelava, Andria, Claudia Schneider, and Nicholas J. Watkins. "The importance of ribosome production, and the 5S RNP–MDM2 pathway, in health and disease." Biochemical Society Transactions 44, no. 4 (2016): 1086–90. http://dx.doi.org/10.1042/bst20160106.

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Ribosomes are abundant, large RNA–protein complexes that are the source of all protein synthesis in the cell. The production of ribosomes is an extremely energetically expensive cellular process that has long been linked to human health and disease. More recently, it has been shown that ribosome biogenesis is intimately linked to multiple cellular signalling pathways and that defects in ribosome production can lead to a wide variety of human diseases. Furthermore, changes in ribosome production in response to nutrient levels in the diet lead to metabolic re-programming of the liver. Reduced or

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Shetty, Sunil, and Umesh Varshney. "An evolutionarily conserved element in initiator tRNAs prompts ultimate steps in ribosome maturation." Proceedings of the National Academy of Sciences 113, no. 41 (2016): E6126—E6134. http://dx.doi.org/10.1073/pnas.1609550113.

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Ribosome biogenesis, a complex multistep process, results in correct folding of rRNAs, incorporation of >50 ribosomal proteins, and their maturation. Deficiencies in ribosome biogenesis may result in varied faults in translation of mRNAs causing cellular toxicities and ribosomopathies in higher organisms. How cells ensure quality control in ribosome biogenesis for the fidelity of its complex function remains unclear. Using Escherichia coli, we show that initiator tRNA (i-tRNA), specifically the evolutionarily conserved three consecutive GC base pairs in its anticodon stem, play a crucial ro

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Tan, Thomas C. J., John Knight, Thomas Sbarrato, Kate Dudek, Anne E. Willis, and Rose Zamoyska. "Suboptimal T-cell receptor signaling compromises protein translation, ribosome biogenesis, and proliferation of mouse CD8 T cells." Proceedings of the National Academy of Sciences 114, no. 30 (2017): E6117—E6126. http://dx.doi.org/10.1073/pnas.1700939114.

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Global transcriptomic and proteomic analyses of T cells have been rich sources of unbiased data for understanding T-cell activation. Lack of full concordance of these datasets has illustrated that important facets of T-cell activation are controlled at the level of translation. We undertook translatome analysis of CD8 T-cell activation, combining polysome profiling and microarray analysis. We revealed that altering T-cell receptor stimulation influenced recruitment of mRNAs to heavy polysomes and translation of subsets of genes. A major pathway that was compromised, when TCR signaling was subo

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Piazzi, Manuela, Alberto Bavelloni, Angela Gallo, Irene Faenza, and William L. Blalock. "Signal Transduction in Ribosome Biogenesis: A Recipe to Avoid Disaster." International Journal of Molecular Sciences 20, no. 11 (2019): 2718. http://dx.doi.org/10.3390/ijms20112718.

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Energetically speaking, ribosome biogenesis is by far the most costly process of the cell and, therefore, must be highly regulated in order to avoid unnecessary energy expenditure. Not only must ribosomal RNA (rRNA) synthesis, ribosomal protein (RP) transcription, translation, and nuclear import, as well as ribosome assembly, be tightly controlled, these events must be coordinated with other cellular events, such as cell division and differentiation. In addition, ribosome biogenesis must respond rapidly to environmental cues mediated by internal and cell surface receptors, or stress (oxidative

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Jiang, M., S. M. Sullivan, A. K. Walker, J. R. Strahler, P. C. Andrews, and J. R. Maddock. "Identification of Novel Escherichia coli Ribosome-Associated Proteins Using Isobaric Tags and Multidimensional Protein Identification Techniques." Journal of Bacteriology 189, no. 9 (2007): 3434–44. http://dx.doi.org/10.1128/jb.00090-07.

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ABSTRACT Biogenesis of the large ribosomal subunit requires the coordinate assembly of two rRNAs and 33 ribosomal proteins. In vivo, additional ribosome assembly factors, such as helicases, GTPases, pseudouridine synthetases, and methyltransferases, are also critical for ribosome assembly. To identify novel ribosome-associated proteins, we used a proteomic approach (isotope tagging for relative and absolute quantitation) that allows for semiquantitation of proteins from complex protein mixtures. Ribosomal subunits were separated by sucrose density centrifugation, and the relevant fractions wer

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Castle, Christopher D., Erica K. Cassimere, Jinho Lee, and Catherine Denicourt. "Las1L Is a Nucleolar Protein Required for Cell Proliferation and Ribosome Biogenesis." Molecular and Cellular Biology 30, no. 18 (2010): 4404–14. http://dx.doi.org/10.1128/mcb.00358-10.

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ABSTRACT Ribosome biogenesis is a highly regulated process ensuring that cell growth (increase in biomass) is coordinated with cell proliferation. The formation of eukaryotic ribosomes is a multistep process initiated by the transcription and processing of rRNA in the nucleolus. Concomitant with this, several preribosomal particles, which transiently associate with numerous nonribosomal factors before mature 60S and 40S subunits are formed and exported in the cytoplasm, are generated. Here we identify Las1L as a previously uncharacterized nucleolar protein required for ribosome biogenesis. Dep

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Jayalath, Kumudie, Sean Frisbie, Minhchau To, and Sanjaya Abeysirigunawardena. "Pseudouridine Synthase RsuA Captures an Assembly Intermediate That Is Stabilized by Ribosomal Protein S17." Biomolecules 10, no. 6 (2020): 841. http://dx.doi.org/10.3390/biom10060841.

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The ribosome is a large ribonucleoprotein complex that synthesizes protein in all living organisms. Ribosome biogenesis is a complex process that requires synchronization of various cellular events, including ribosomal RNA (rRNA) transcription, ribosome assembly, and processing and post-transcriptional modification of rRNA. Ribosome biogenesis is fine-tuned with various assembly factors, possibly including nucleotide modification enzymes. Ribosomal small subunit pseudouridine synthase A (RsuA) pseudouridylates U516 of 16S helix 18. Protein RsuA is a multi-domain protein that contains the N-ter

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Saurer, Martin, David J. F. Ramrath, Moritz Niemann, et al. "Mitoribosomal small subunit biogenesis in trypanosomes involves an extensive assembly machinery." Science 365, no. 6458 (2019): 1144–49. http://dx.doi.org/10.1126/science.aaw5570.

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Mitochondrial ribosomes (mitoribosomes) are large ribonucleoprotein complexes that synthesize proteins encoded by the mitochondrial genome. An extensive cellular machinery responsible for ribosome assembly has been described only for eukaryotic cytosolic ribosomes. Here we report that the assembly of the small mitoribosomal subunit in Trypanosoma brucei involves a large number of factors and proceeds through the formation of assembly intermediates, which we analyzed by using cryo–electron microscopy. One of them is a 4-megadalton complex, referred to as the small subunit assemblosome, in which

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Lejars, Maxence, Asaki Kobayashi, and Eliane Hajnsdorf. "RNase III, Ribosome Biogenesis and Beyond." Microorganisms 9, no. 12 (2021): 2608. http://dx.doi.org/10.3390/microorganisms9122608.

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The ribosome is the universal catalyst for protein synthesis. Despite extensive studies, the diversity of structures and functions of this ribonucleoprotein is yet to be fully understood. Deciphering the biogenesis of the ribosome in a step-by-step manner revealed that this complexity is achieved through a plethora of effectors involved in the maturation and assembly of ribosomal RNAs and proteins. Conserved from bacteria to eukaryotes, double-stranded specific RNase III enzymes play a large role in the regulation of gene expression and the processing of ribosomal RNAs. In this review, we desc

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Scull, Catherine E., Guy Twa, Yinfeng Zhang, et al. "Small Molecule RBI2 Disrupts Ribosome Biogenesis through Pre-rRNA Depletion." Cancers 15, no. 13 (2023): 3303. http://dx.doi.org/10.3390/cancers15133303.

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Cancer cells are especially sensitive to perturbations in ribosome biogenesis as they rely on finely tuned protein homeostasis to facilitate their rapid growth and proliferation. While ribosome synthesis and cancer have a well-established relationship, ribosome biogenesis has only recently drawn interest as a cancer therapeutic target. In this study, we exploited the relationship between ribosome biogenesis and cancer cell proliferation by using a potent ribosome biogenesis inhibitor, RBI2 (Ribosome Biogenesis Inhibitor 2), to perturb cancer cell growth and viability. We demonstrate herein tha

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Iouk, Tatiana L., John D. Aitchison, Shawna Maguire, and Richard W. Wozniak. "Rrb1p, a Yeast Nuclear WD-Repeat Protein Involved in the Regulation of Ribosome Biosynthesis." Molecular and Cellular Biology 21, no. 4 (2001): 1260–71. http://dx.doi.org/10.1128/mcb.21.4.1260-1271.2001.

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ABSTRACT Ribosome biogenesis is regulated by environmental cues that coordinately modulate the synthesis of ribosomal components and their assembly into functional subunits. We have identified an essential yeast WD-repeat-containing protein, termed Rrb1p, that has a role in both the assembly of the 60S ribosomal subunits and the transcriptional regulation of ribosomal protein (RP) genes. Rrb1p is located in the nucleus and is concentrated in the nucleolus. Its presence is required to maintain normal cellular levels of 60S subunits, 80S ribosomes, and polyribosomes. The function of Rrb1p in rib

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Cottilli, Patrick, Borja Belda-Palazón, Charith Raj Adkar-Purushothama, et al. "Citrus exocortis viroid causes ribosomal stress in tomato plants." Nucleic Acids Research 47, no. 16 (2019): 8649–61. http://dx.doi.org/10.1093/nar/gkz679.

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Abstract Viroids are naked RNAs that do not code for any known protein and yet are able to infect plants causing severe diseases. Because of their RNA nature, many studies have focused on the involvement of viroids in RNA-mediated gene silencing as being their pathogenesis mechanism. Here, the alterations caused by the Citrus exocortis viroid (CEVd) on the tomato translation machinery were studied as a new aspect of viroid pathogenesis. The presence of viroids in the ribosomal fractions of infected tomato plants was detected. More precisely, CEVd and its derived viroid small RNAs were found to

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Firmino, Alexandre Augusto Pereira, Michal Gorka, Alexander Graf, et al. "Separation and Paired Proteome Profiling of Plant Chloroplast and Cytoplasmic Ribosomes." Plants 9, no. 7 (2020): 892. http://dx.doi.org/10.3390/plants9070892.

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Conventional preparation methods of plant ribosomes fail to resolve non-translating chloroplast or cytoplasmic ribosome subunits from translating fractions. We established preparation of these ribosome complexes from Arabidopsis thaliana leaf, root, and seed tissues by optimized sucrose density gradient centrifugation of protease protected plant extracts. The method co-purified non-translating 30S and 40S ribosome subunits separated non-translating 50S from 60S subunits, and resolved assembled monosomes from low oligomeric polysomes. Combining ribosome fractionation with microfluidic rRNA anal

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Dong, Jinsheng, Ruby Lai, Jennifer L. Jennings, Andrew J. Link, and Alan G. Hinnebusch. "The Novel ATP-Binding Cassette Protein ARB1 Is a Shuttling Factor That Stimulates 40S and 60S Ribosome Biogenesis." Molecular and Cellular Biology 25, no. 22 (2005): 9859–73. http://dx.doi.org/10.1128/mcb.25.22.9859-9873.2005.

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ABSTRACT ARB1 is an essential yeast protein closely related to members of a subclass of the ATP-binding cassette (ABC) superfamily of proteins that are known to interact with ribosomes and function in protein synthesis or ribosome biogenesis. We show that depletion of ARB1 from Saccharomyces cerevisiae cells leads to a deficit in 18S rRNA and 40S subunits that can be attributed to slower cleavage at the A0, A1, and A2 processing sites in 35S pre-rRNA, delayed processing of 20S rRNA to mature 18S rRNA, and a possible defect in nuclear export of pre-40S subunits. Depletion of ARB1 also delays rR

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Gamerdinger, Martin. "Protein quality control at the ribosome: focus on RAC, NAC and RQC." Essays in Biochemistry 60, no. 2 (2016): 203–12. http://dx.doi.org/10.1042/ebc20160011.

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The biogenesis of new polypeptides by ribosomes and their subsequent correct folding and localization to the appropriate cellular compartments are essential key processes to maintain protein homoeostasis. These complex mechanisms are governed by a repertoire of protein biogenesis factors that directly bind to the ribosome and chaperone nascent polypeptide chains as soon as they emerge from the ribosomal tunnel exit. This nascent chain ‘welcoming committee’ regulates multiple co-translational processes including protein modifications, folding, targeting and degradation. Acting at the front of t

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De, Sandip, and Saverio Brogna. "Are ribosomal proteins present at transcription sites on or off ribosomal subunits?" Biochemical Society Transactions 38, no. 6 (2010): 1543–47. http://dx.doi.org/10.1042/bst0381543.

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RPs (ribosomal proteins) are main components of the ribosome having essential functions in its biogenesis, function and structural integrity. Although most of the RP molecules are in the cytoplasm, being incorporated into translating ribosomes, some RPs have non-ribosomal functions when they are off ribosomal subunits. Notably, in eukaryotes, RPs are also present at transcription sites and some of these proteins have a function in transcription and pre-mRNA processing of specific genes. Although the consensus is that the proteins found at these sites are isolated RPs not assembled into ribosom

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Martinez-Seidel, Federico, Olga Beine-Golovchuk, Yin-Chen Hsieh, et al. "Spatially Enriched Paralog Rearrangements Argue Functionally Diverse Ribosomes Arise during Cold Acclimation in Arabidopsis." International Journal of Molecular Sciences 22, no. 11 (2021): 6160. http://dx.doi.org/10.3390/ijms22116160.

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Ribosome biogenesis is essential for plants to successfully acclimate to low temperature. Without dedicated steps supervising the 60S large subunits (LSUs) maturation in the cytosol, e.g., Rei-like (REIL) factors, plants fail to accumulate dry weight and fail to grow at suboptimal low temperatures. Around REIL, the final 60S cytosolic maturation steps include proofreading and assembly of functional ribosomal centers such as the polypeptide exit tunnel and the P-Stalk, respectively. In consequence, these ribosomal substructures and their assembly, especially during low temperatures, might be ch

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Scull, Catherine E., Yinfeng Zhang, Nichole Tower, et al. "Discovery of novel inhibitors of ribosome biogenesis by innovative high throughput screening strategies." Biochemical Journal 476, no. 15 (2019): 2209–19. http://dx.doi.org/10.1042/bcj20190207.

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Abstract Over the past two decades, ribosome biogenesis has emerged as an attractive target for cancer treatment. In this study, two high-throughput screens were used to identify ribosome biogenesis inhibitors. Our primary screen made use of the HaloTag selective labeling strategy to identify compounds that decreased the abundance of newly synthesized ribosomes in A375 malignant melanoma cells. This screen identified 5786 hit compounds. A subset of those initial hit compounds were tested using a secondary screen that directly measured pre-ribosomal RNA (pre-rRNA) abundance as a reporter of rRN

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