WordNet
- slight or limited; especially in degree or intensity or scope; "a series of death struggles with small time in between"
- a garment size for a small person
- the slender part of the back
- limited or below average in number or quantity or magnitude or extent; "a little dining room"; "a little house"; "a small car"; "a little (or small) group" (同)little
- have fine or very small constituent particles; "a small misty rain"
- on a small scale; "think small"
- an organelle in the cytoplasm of a living cell; they attach to mRNA and move down it one codon at a time and then stop until tRNA brings the required amino acid; when it reaches a stop codon it falls apart and releases the completed protein molecule for u
PrepTutorEJDIC
- (大きさが)『小さい』,小形の;(量が)『少ない』,わずかな / 『取るに足りない』,ささいな(trivial) / 《名詞の前にのみ用いて》(仕事・活動などが)『小規模の』,ささやかな / 心が狭い,利己的な / (音・声が)弱い,小さい / (文字が)小型の,小文字の / 《the~》小さいもの;(…の)細い部分《+『of』+『名』》 / 《複数形で》《英》(衣類・ハンカチなどの)小物,小間物 / 小さく,細かく / (声などが)低く,弱く / 小規模に,こぢんまりと
- リボゾーム(細胞質に含まれ,蛋白質とリボ核酸から成る微小粒子)
UpToDate Contents
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English Journal
- Eukaryotic ribosomal protein S3: A constituent of translational machinery and an extraribosomal player in various cellular processes.
- Graifer D1, Malygin A2, Zharkov DO1, Karpova G3.Author information 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, 630090 Novosibirsk, Russia; Department of Natural Sciences, Novosibirsk State University, ul. Pirogova, 2, 630090 Novosibirsk, Russia.2Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, 630090 Novosibirsk, Russia.3Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, 630090 Novosibirsk, Russia. Electronic address: karpova@niboch.nsc.ru.AbstractRibosomal proteins from the S3 family are universal components of small ribosomal subunits in all three domains of life. In eukaryotes, ribosomal protein S3e (rpS3e) is one of 33 proteins of small subunit of the ribosome. It functions not only within the ribosome participating in translation but also as an extraribosomal player involved in a number of vitally important cellular events. RpS3e is directly implicated in translation initiation via participation in rearrangements of the small subunit structure occurring upon the binding of initiation factors eIF1 and eIF1A, which opens the ribosomal mRNA binding channel for incoming mRNA and allows scanning. Being located at the mRNA entry site of the ribosome, rpS3e is suggested to interact with mRNA part downstream of the codon at the decoding site and it could be implicated in helicase activity of the ribosome by analogy to its bacterial counterpart rpS3p. Extraribosomal functions of rpS3e are mainly based on its ability to bind to nucleic acids, although protein-protein interactions take place too. As an independent player, rpS3e is involved in DNA repair, selective gene regulation via implication in NF-κB signaling pathway, inducing apoptosis, control of expression of the own gene at the translation level and molecular interactions affecting half-life of the protein. Involvement of rpS3e in various cellular processes is mediated by specific mechanisms utilizing post-translational modifications of the protein. Here, we present accumulated to date information and current ideas concerning functions of rpS3e as a constituent of translational machinery and of the free protein as a key player in various events of the cell life.
- Biochimie.Biochimie.2014 Apr;99C:8-18. doi: 10.1016/j.biochi.2013.11.001. Epub 2013 Nov 13.
- Ribosomal proteins from the S3 family are universal components of small ribosomal subunits in all three domains of life. In eukaryotes, ribosomal protein S3e (rpS3e) is one of 33 proteins of small subunit of the ribosome. It functions not only within the ribosome participating in translation but als
- PMID 24239944
- GTP hydrolysis by EF-G synchronizes tRNA movement on small and large ribosomal subunits.
- Holtkamp W1, Cunha CE, Peske F, Konevega AL, Wintermeyer W, Rodnina MV.Author information 1Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.AbstractElongation factor G (EF-G) promotes the movement of two tRNAs and the mRNA through the ribosome in each cycle of peptide elongation. During translocation, the tRNAs transiently occupy intermediate positions on both small (30S) and large (50S) ribosomal subunits. How EF-G and GTP hydrolysis control these movements is still unclear. We used fluorescence labels that specifically monitor movements on either 30S or 50S subunits in combination with EF-G mutants and translocation-specific antibiotics to investigate timing and energetics of translocation. We show that EF-G-GTP facilitates synchronous movements of peptidyl-tRNA on the two subunits into an early post-translocation state, which resembles a chimeric state identified by structural studies. EF-G binding without GTP hydrolysis promotes only partial tRNA movement on the 50S subunit. However, rapid 30S translocation and the concomitant completion of 50S translocation require GTP hydrolysis and a functional domain 4 of EF-G. Our results reveal two distinct modes for utilizing the energy of EF-G binding and GTP hydrolysis and suggest that coupling of GTP hydrolysis to translocation is mediated through rearrangements of the 30S subunit.
- The EMBO journal.EMBO J.2014 Mar 10. [Epub ahead of print]
- Elongation factor G (EF-G) promotes the movement of two tRNAs and the mRNA through the ribosome in each cycle of peptide elongation. During translocation, the tRNAs transiently occupy intermediate positions on both small (30S) and large (50S) ribosomal subunits. How EF-G and GTP hydrolysis control t
- PMID 24614227
- Drosophila Mbm is a Nucleolar Myc and CK2 Target Required for Ribosome Biogenesis and Cell Growth of Central Brain Neuroblasts.
- Hovhanyan A1, Herter EK, Pfannstiel J, Gallant P, Raabe T.Author information 1University of Würzburg, Institute for Medical Radiation and Cell Research, Versbacherstr. 5, D-97078 Würzburg, Germany.AbstractProper cell growth is a prerequisite for maintaining repeated cell divisions. Cells need to translate information about intracellular nutrient availability and growth cues from energy sensing organs into growth promoting processes such as the sufficient supply with ribosomes for protein synthesis. Mutations in the mushroom body miniature (mbm) gene impair proliferation of neural progenitor cells (neuroblasts) in the central brain of Drosophila. Yet, the molecular function of Mbm has been unknown so far. Here we show that mbm does not affect the molecular machinery controlling asymmetric cell division of neuroblasts but instead decreases their cell size. Mbm is a nucleolar protein required for small ribosomal subunit biogenesis in neuroblasts. Accordingly, levels of protein synthesis are reduced in mbm neuroblasts. Mbm expression is transcriptionally regulated by Myc, which among other functions relays information from nutrient dependent signaling pathways to ribosomal gene expression. At the posttranslational level, Mbm becomes phosphorylated by protein kinase CK2, which has an impact on localization of the protein. We conclude that Mbm is a new part of the Myc target network involved in ribosome biogenesis, which together with CK2-mediated signals enables neuroblasts to synthesize sufficient amounts of proteins required for proper cell growth.
- Molecular and cellular biology.Mol Cell Biol.2014 Mar 10. [Epub ahead of print]
- Proper cell growth is a prerequisite for maintaining repeated cell divisions. Cells need to translate information about intracellular nutrient availability and growth cues from energy sensing organs into growth promoting processes such as the sufficient supply with ribosomes for protein synthesis. M
- PMID 24615015
Japanese Journal
- Functional Study of the Residue C899 in the 900 Tetraloop of Escherichia coli Small Subunit Ribosomal RNA
- HA Hye-Jeong,SONG Woo-Seok,KIM Hong-Man,SON Ho-Sun,LEE Kangseok
- Bioscience, biotechnology, and biochemistry 73(11), 2544-2546, 2009-11-23
- … A mutant ribosome bearing C899G in the 900 tetraloop of Escherichia coli 16S rRNA, one implicated in a conformational switch in the dynamic movements of the ribosome, showed defects in subunit association and 30S initiation complex formation. …
- NAID 10027548302
- 近藤 次郎
- 日本結晶学会誌 51(2), 145-152, 2009-04-30
- … The aminoacyl-tRNA decoding site (A-site) on the small ribosomal subunit is an RNA molecular switch guaranteeing high translation fidelity. … However, these three cell types are noticeably different in their biological properties such as life cycle, genome size, structural component of ribosome and number of tRNA species. …
- NAID 10024820582
- Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome : identification of a novel s1 domain-containing protein and unusually large orthologs of bacterial S2, S3 and S5
Related Links
- The structure of the large subunit is available in PDB entry 1ffk . The large subunit contains the active site of the ribosome: the site that creates the new peptide bonds when proteins are synthesized. In this view, the messenger RNA ...
- Small subunit ribosomal RNA, 5' domain explanation free. What is Small subunit ribosomal RNA, 5' domain? Meaning of Small subunit ribosomal RNA, 5' domain medical term. What does Small subunit ribosomal Small subunit ...
Related Pictures
★リンクテーブル★
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- 英
- small ribosome subunit
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- 関
- little、petit、tiny
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- 関
- ribosomal subunit