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Relevant bibliographies by topics / Large ribosomal subunit

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Academic literature on the topic 'Large ribosomal subunit'

Author: Grafiati

Published: 7 September 2022

Last updated: 31 July 2025

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Journal articles on the topic "Large ribosomal subunit"

1

Siibak, Triinu, Lauri Peil, Liqun Xiong, Alexander Mankin, Jaanus Remme, and Tanel Tenson. "Erythromycin- and Chloramphenicol-Induced Ribosomal Assembly Defects Are Secondary Effects of Protein Synthesis Inhibition." Antimicrobial Agents and Chemotherapy 53, no. 2 (2008): 563–71. http://dx.doi.org/10.1128/aac.00870-08.

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ABSTRACT Several protein synthesis inhibitors are known to inhibit ribosome assembly. This may be a consequence of direct binding of the antibiotic to ribosome precursor particles, or it could result indirectly from loss of coordination in the production of ribosomal components due to the inhibition of protein synthesis. Here we demonstrate that erythromycin and chloramphenicol, inhibitors of the large ribosomal subunit, affect the assembly of both the large and small subunits. Expression of a small erythromycin resistance peptide acting in cis on mature ribosomes relieves the erythromycin-med

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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

Petrov, Anton S., Burak Gulen, Ashlyn M. Norris, et al. "History of the ribosome and the origin of translation." Proceedings of the National Academy of Sciences 112, no. 50 (2015): 15396–401. http://dx.doi.org/10.1073/pnas.1509761112.

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We present a molecular-level model for the origin and evolution of the translation system, using a 3D comparative method. In this model, the ribosome evolved by accretion, recursively adding expansion segments, iteratively growing, subsuming, and freezing the rRNA. Functions of expansion segments in the ancestral ribosome are assigned by correspondence with their functions in the extant ribosome. The model explains the evolution of the large ribosomal subunit, the small ribosomal subunit, tRNA, and mRNA. Prokaryotic ribosomes evolved in six phases, sequentially acquiring capabilities for RNA f

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4

Aoyama, Ryo, Keiko Masuda, Masaru Shimojo, Takashi Kanamori, Takuya Ueda, and Yoshihiro Shimizu. "In vitro reconstitution of the Escherichia coli 70S ribosome with a full set of recombinant ribosomal proteins." Journal of Biochemistry 171, no. 2 (2021): 227–37. http://dx.doi.org/10.1093/jb/mvab121.

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Abstract Many studies of the reconstitution of the Escherichia coli small ribosomal subunit from its individual molecular parts have been reported, but contrastingly, similar studies of the large ribosomal subunit have not been well performed to date. Here, we describe protocols for preparing the 33 ribosomal proteins of the E. coli 50S subunit and demonstrate successful reconstitution of a functionally active 50S particle that can perform protein synthesis in vitro. We also successfully reconstituted both ribosomal subunits (30S and 50S) and 70S ribosomes using a full set of recombinant ribos

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5

Moy, Terence I., and Pamela A. Silver. "Requirements for the nuclear export of the small ribosomal subunit." Journal of Cell Science 115, no. 14 (2002): 2985–95. http://dx.doi.org/10.1242/jcs.115.14.2985.

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Eukaryotic ribosome biogenesis requires multiple steps of nuclear transport because ribosomes are assembled in the nucleus while protein synthesis occurs in the cytoplasm. Using an in situ RNA localization assay in the yeast Saccharomyces cerevisiae, we determined that efficient nuclear export of the small ribosomal subunit requires Yrb2, a factor involved in Crm1-mediated export. Furthermore, in cells lacking YRB2, the stability and abundance of the small ribosomal subunit is decreased in comparison with the large ribosomal subunit. To identify additional factors affecting small subunit expor

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Ling, Clarence, and Dmitri N. Ermolenko. "Initiation factor 2 stabilizes the ribosome in a semirotated conformation." Proceedings of the National Academy of Sciences 112, no. 52 (2015): 15874–79. http://dx.doi.org/10.1073/pnas.1520337112.

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Intersubunit rotation and movement of the L1 stalk, a mobile domain of the large ribosomal subunit, have been shown to accompany the elongation cycle of translation. The initiation phase of protein synthesis is crucial for translational control of gene expression; however, in contrast to elongation, little is known about the conformational rearrangements of the ribosome during initiation. Bacterial initiation factors (IFs) 1, 2, and 3 mediate the binding of initiator tRNA and mRNA to the small ribosomal subunit to form the initiation complex, which subsequently associates with the large subuni

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Jiang, Mengxi, Kaustuv Datta, Angela Walker, et al. "The Escherichia coli GTPase CgtAE Is Involved in Late Steps of Large Ribosome Assembly." Journal of Bacteriology 188, no. 19 (2006): 6757–70. http://dx.doi.org/10.1128/jb.00444-06.

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ABSTRACT The bacterial ribosome is an extremely complicated macromolecular complex the in vivo biogenesis of which is poorly understood. Although several bona fide assembly factors have been identified, their precise functions and temporal relationships are not clearly defined. Here we describe the involvement of an Escherichia coli GTPase, CgtAE, in late steps of large ribosomal subunit biogenesis. CgtAE belongs to the Obg/CgtA GTPase subfamily, whose highly conserved members are predominantly involved in ribosome function. Mutations in CgtAE cause both polysome and rRNA processing defects; s

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8

Stern, Seth, and Prakash Purohit. "An oligonucleotide analog approach to the decoding region of 16S rRNA." Biochemistry and Cell Biology 73, no. 11-12 (1995): 899–905. http://dx.doi.org/10.1139/o95-097.

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Despite the passage of about 30 years since the discovery of the translational activities of ribosomes and the outlining of the roles of the large and small subunits, the actual molecular basis for the mRNA decoding activities of the small subunit has remained essentially obscure. In this paper, we describe a new approach using oligonucleotide analogs of 16S ribosomal RNA, in which the small ribosomal subunit is effectively deconstructed into a smaller more experimentally tractable form. Specifically, we review the results of experiments using an oligonucleotide analog of the decoding region o

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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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Gadal, Olivier, Daniela Strauß, Jacques Kessl, Bernard Trumpower, David Tollervey, and Ed Hurt. "Nuclear Export of 60S Ribosomal Subunits Depends on Xpo1p and Requires a Nuclear Export Sequence-Containing Factor, Nmd3p, That Associates with the Large Subunit Protein Rpl10p." Molecular and Cellular Biology 21, no. 10 (2001): 3405–15. http://dx.doi.org/10.1128/mcb.21.10.3405-3415.2001.

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ABSTRACT Nuclear export of ribosomes requires a subset of nucleoporins and the Ran system, but specific transport factors have not been identified. Using a large subunit reporter (Rpl25p-eGFP), we have isolated several temperature-sensitive ribosomal export (rix) mutants. One of these corresponds to the ribosomal protein Rpl10p, which interacts directly with Nmd3p, a conserved and essential protein associated with 60S subunits. We find that thermosensitive nmd3 mutants are impaired in large subunit export. Strikingly, Nmd3p shuttles between the nucleus and cytoplasm and is exported by the nucl

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Dissertations / Theses on the topic "Large ribosomal subunit"

1

Oristian, Daniel S. "Skeletal phenotype of mice lacking HIP/RPL29, a component of the large ribosomal subunit." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 70 p, 2007. http://proquest.umi.com/pqdweb?did=1397900441&sid=6&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Ho, Hei Ngam Jennifer. "Functional characterization of yeast NMD3 in the biogenesis and transport of the large (60S) ribosomal subunit /." Full text (PDF) from UMI/Dissertation Abstracts International, 2000. http://wwwlib.umi.com/cr/utexas/fullcit?p3004287.

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Ohmayer, Uli [Verfasser], and Herbert [Akademischer Betreuer] Tschochner. "Studies on the assembly process of large subunit ribosomal proteins in S.cerevisiae / Uli Ohmayer. Betreuer: Herbert Tschochner." Regensburg : Universitätsbibliothek Regensburg, 2014. http://d-nb.info/1077095961/34.

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Hurtado, Ana Isabel. "Large-subunit ribosomal RNA gene of Helicobacter and Campylobacter species : its role in genotypic identification and typing." Thesis, Queen Mary, University of London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.265831.

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Saini, Jagmohan [Verfasser]. "Structural and dynamic insights into oxazolidinone binding, selectivity and resistance to the large ribosomal subunit / Jagmohan Saini." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2018. http://d-nb.info/1154307018/34.

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Khreiss, Ali. "Dbp6, une ARN hélicase requise pour les étapes précoces de la synthèse de la grande sous-unité du ribosome eucaryotes." Thesis, Toulouse 3, 2022. http://www.theses.fr/2022TOU30061.

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L'activité de traduction des ribosomes est portée directement par les ARN ribosomiques (ARNr) qui composent ses deux sous-unités. La grande sous-unité (60S) est formée par les ARNr 25S, 5.8S et 5S et la petite sous-unité (40S) est formée par l'ARNr 18S. Un des principaux buts de la biogenèse des ribosomes est de convertir les ARNr en molécules correctement repliées et donc actives. La production des sous-unités ribosomiques est le résultat d'étapes successives de maturation de particules précurseurs, les pré-60S et les pré-40S, précurseurs de la grande (60S) et la petite (40S) sous-unité ribos

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Aime, Mary Catherine. "Generic concepts in the Crepidotaceae as inferred from nuclear large subunit ribosomal DNA sequences, morphology, and basidiospore dormancy patterns." Thesis, Virginia Tech, 1998. http://hdl.handle.net/10919/32285.

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The Crepidotaceae (Imai) Singer (Basidiomycetes: Agaricales) represents a proposed family of saprophytic fungi containing five agaricoid (Crepidotus, Tubaria, Melanomphalia, Simocybe, Pleurotellus) and four cyphelloid (Episphaeria, Phaeosolenia, Pellidiscus, Chromocyphella) genera. Several contemporary classification systems exist that delegate some or all of these genera to other agaric families. Phylogenetic relationships for the most prevalent genera in the Crepidotaceae were investigated using nuclear large subunit ribosomal DNA (LSU rDNA) sequences. Parsimony analysis of the molecular dat

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Teubl, Fabian [Verfasser], and Joachim [Akademischer Betreuer] Griesenbeck. "Structural and Functional Studies on the Role of Noc3p for Large Ribosomal Subunit Maturation in Saccharomyces cerevisiae / Fabian Teubl ; Betreuer: Joachim Griesenbeck." Regensburg : Universitätsbibliothek Regensburg, 2020. http://d-nb.info/1223198138/34.

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Gamalinda, Michael. "Ribosomal Proteins Orchestrate the Biogenesis of Eukaryotic Large Ribosomal Subunits in a Sequential Fashion." Research Showcase @ CMU, 2014. http://repository.cmu.edu/dissertations/441.

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Ribosome biogenesis in eukaryotes involves the transcription, folding, and processing of ribosomal RNA (rRNA), as well as the concomitant assembly of ribosomal proteins. Several hundred trans-acting assembly factors also play a role in the complex process of ribosome biogenesis. Investigations of the construction of ribosomes have focused primarily on the roles of these assembly factors. Little is understood about how ribosomal proteins (r-proteins) function in ribosomal subunit biogenesis in vivo, in either prokaryotes or eukaryotes. I began by focusing on a subset of r-proteins surrounding t

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Kaminishi, Tatsuya, Andreas Schedlbauer, Attilio Fabbretti, et al. "Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A." Oxford University Press, 2015. http://hdl.handle.net/10757/608247.

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Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its

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Books on the topic "Large ribosomal subunit"

1

Humpert, Andrea J. Systematics of the genus Ramaria inferred from nuclear large subunit and mitochondrial small subunit ribosomal DNA sequences. 1999.

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Grubisha, Lisa C. Systematics of the genus Rhizopogon inferred from nuclear ribosomal DNA large subunit and internal transcribed spacer sequences. 1998.

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3

Amberg, Sean M. Nucleotide sequence of two chloroplast genes from a Chlorella-like green alga: The large subunit of Ribulose-1,5-bisphosphate carboxylase/oxygenase and ribosomal protein S14. 1989.

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Book chapters on the topic "Large ribosomal subunit"

1

Ludwig, W. "Structure and Phylogenetic Information of Large Subunit Ribosomal RNA." In Studies in Classification, Data Analysis, and Knowledge Organization. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-46757-8_30.

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Ban, Nenad, Poul Nissen, Peter B. Moore, and Thomas A. Steitz. "Crystal Structure of the Large Ribosomal Subunit at 5-Angstrom Resolution." In The Ribosome. ASM Press, 2014. http://dx.doi.org/10.1128/9781555818142.ch2.

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Barbet-Massin, Emeline, Eli van der Sluis, Joanna Musial, Roland Beckmann, and Bernd Reif. "Reconstitution of Isotopically Labeled Ribosomal Protein L29 in the 50S Large Ribosomal Subunit for Solution-State and Solid-State NMR." In Protein Complex Assembly. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7759-8_6.

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Cavener, Douglas R., and Beth A. Cavener. "Translation Start Sites and mRNA Leaders." In An Atlas of Drosophila Genes. Oxford University PressNew York, NY, 1993. http://dx.doi.org/10.1093/oso/9780195071160.003.0036.

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Abstract A prototypical eukaryotic mRNA is often described as having a short (less than 100 nt) 5’ untranslated leader sequence upstream of start codon containing a good consensus sequence (Lewin 1990). Translation initiation from such a mRNA follows the scanning model whereby: (1) a complex of proteins including the cap-binding protein (eIF-4E) associates with the 5’ cap of the mRNA; (2) this complex in turn facilitates binding of the preinitiation complex (40S ribosomal subunits + eIF-2-GTP-tRNAmet); (3) the preinitiation complex scans the mRNA searching for the start codon (the first AUG en

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5

Maroni, Gustavo. "Ribosomal Protein 49: Rp49." In An Atlas of Drosophila Genes. Oxford University PressNew York, NY, 1993. http://dx.doi.org/10.1093/oso/9780195071160.003.0026.

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Abstract Protein 49 of the large ribosomal subunit (Vaslet et al. 1980; O’Connell and Rosbash 1984). The syntheses of ribosomal proteins are coordinately regulated and at least part of that regulation occurs at the level of translation. For instance, while almost all Rp49 mRNA is translated during oogenesis, only a small fraction is associated with polysomes early in embryogenesis (Al-Atia et al. 1985).

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Chen, R., and D. Fink. "Computing the Structure of Large Complexes: Modeling the 16S Ribosoma RNA." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0025.

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Ribosomes are the sites of messenger RNA (mRNA) translation to protein, and thus are crucial to the normal functioning of all cells. These ribonucleoprotein particles are composed of a small (30S) subunit and a large (50S) subunit. The 30S subunit, in turn, is composed of a strand of RNA (16S rRNA) and 21 proteins ranging in molecular weight from 9 kD to 61 kD. Studies have demonstrated that ribosomal RNA is necessary for normal ribosome function and protein production (Dahlberg, 1989; Noller, 1991). In particular, 16S rRNA is essential for normal assembly and function of the 30S subunit, whic

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Elliott, David, and Michael Ladomery. "Translation of messenger RNA." In Molecular Biology of RNA. Oxford University Press, 2015. http://dx.doi.org/10.1093/hesc/9780199671397.003.00011.

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This chapter covers the process of mRNA translation. Itbegins by reviewing the structure and function of the essential machinery of translation, namely the ribosome and transfer RNA. The chapter outlines the three phases of translation: initiation, elongation, and termination. It also discusses several ways in which mRNA translation can be regulated. The chapter details how ribosomes catalyse the synthesis of polypeptide chains that form when amino acids are covalently linked through peptide bonds. The chapter explains that ribosomes are made up of large and small subunits that contain ribosom

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Medlin*, L. K., G. L. A. Barkert†, M. Baumann*, P. K. Hayest†, and M. Lange*. "Molecular biology and systematics." In The Haptophyte Algae. Oxford University PressOxford, 1994. http://dx.doi.org/10.1093/oso/9780198577720.003.0021.

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Abstract Sequence data from both the nuclear and plastid encoded small subunit ribosomal RNA (ssu rRNA) gene have been used to infer the phylogenetic position of the haptophyte host cell and its plastid. Both are in distinct lineages that do not share a recent evolutionary history with their chromophyte counterparts. Within the haptophyte lineage ssu rRNA sequence data support the recognition of at least three colony forming species within the ubiquitous genus, Phaeocystis. In contrast, the two distinct morphotypes of the cosmopolitan bloom-forming coccolithophorid, Emiliania huxleyi, are iden

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Nissen, Poul, Joseph A. Ippolito, Nenad Ban, Peter B. Moore, and Thomas A. Steitz. "RNA tertiary interactions in the large ribosomal subunit: The A-minor motif." In Structural Insights into Gene Expression and Protein Synthesis. WORLD SCIENTIFIC, 2020. http://dx.doi.org/10.1142/9789811215865_0061.

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Hansen, Jeffrey L., Joseph A. Ippolito, Nenad Ban, Poul Nissen, Peter B. Moore, and Thomas A. Steitz. "The Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit." In Structural Insights into Gene Expression and Protein Synthesis. WORLD SCIENTIFIC, 2020. http://dx.doi.org/10.1142/9789811215865_0063.

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Reports on the topic "Large ribosomal subunit"

1

Ostersetzer-Biran, Oren, and Jeffrey Mower. Novel strategies to induce male sterility and restore fertility in Brassicaceae crops. United States Department of Agriculture, 2016. http://dx.doi.org/10.32747/2016.7604267.bard.

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Abstract Mitochondria are the site of respiration and numerous other metabolic processes required for plant growth and development. Increased demands for metabolic energy are observed during different stages in the plants life cycle, but are particularly ample during germination and reproductive organ development. These activities are dependent upon the tight regulation of the expression and accumulation of various organellar proteins. Plant mitochondria contain their own genomes (mtDNA), which encode for rRNAs, tRNAs and some mitochondrial proteins. Although all mitochondria have probably evo

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