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[PMID]:29215639
[Au] Autor:Noller HF; Lancaster L; Zhou J; Mohan S
[Ad] Endereço:Department of Molecular, Cell and Developmental Biology and Center for Molecular Biology of RNA, University of California at Santa Cruz, Santa Cruz, California, USA.
[Ti] Título:The ribosome moves: RNA mechanics and translocation.
[So] Source:Nat Struct Mol Biol;24(12):1021-1027, 2017 Dec 07.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During protein synthesis, mRNA and tRNAs must be moved rapidly through the ribosome while maintaining the translational reading frame. This process is coupled to large- and small-scale conformational rearrangements in the ribosome, mainly in its rRNA. The free energy from peptide-bond formation and GTP hydrolysis is probably used to impose directionality on those movements. We propose that the free energy is coupled to two pawls, namely tRNA and EF-G, which enable two ratchet mechanisms to act separately and sequentially on the two ribosomal subunits.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Biossíntese de Proteínas/fisiologia
RNA Mensageiro/genética
RNA de Transferência/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Bactérias/genética
Modelos Moleculares
Fator G para Elongação de Peptídeos/metabolismo
Conformação Proteica
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (RNA, Messenger); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3505


  2 / 567 MEDLINE  
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[PMID]:29211986
[Au] Autor:Jamiolkowski RM; Chen C; Cooperman BS; Goldman YE
[Ad] Endereço:Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania.
[Ti] Título:tRNA Fluctuations Observed on Stalled Ribosomes Are Suppressed during Ongoing Protein Synthesis.
[So] Source:Biophys J;113(11):2326-2335, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pretranslocation complex of the ribosome can undergo spontaneous fluctuations of messenger RNA and transfer RNAs (tRNAs) between classical and hybrid states, and occupation of the hybrid tRNA positions has been proposed to precede translocation. The classical and hybrid state tRNA positions have been extensively characterized when the ribosome is stalled along the messenger RNA by either the absence or delayed addition of elongation factor G (EF-G), or by the presence of antibiotics or GTP analogs that block translocation. However, during multiple ongoing elongation cycles when both EF-G and ternary complexes are present, EF-G can bind to the pretranslocation complex much faster than the timescale of the classic-hybrid transitions. Using single-molecule fluorescence resonance energy transfer between adjacent tRNAs and between A-site tRNA and ribosomal protein L11, we found that the tRNAs do not fluctuate between the hybrid and classical states, but instead adopt a position with fluorescence resonance energy transfer efficiencies between those of the stalled classical and hybrid states.
[Mh] Termos MeSH primário: Biossíntese de Proteínas
RNA de Transferência/genética
Ribossomos/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Fator G para Elongação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Ribosomal Proteins); 0 (ribosomal protein L11); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  3 / 567 MEDLINE  
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[PMID]:28934499
[Au] Autor:Almutairi MM; Svetlov MS; Hansen DA; Khabibullina NF; Klepacki D; Kang HY; Sherman DH; Vázquez-Laslop N; Polikanov YS; Mankin AS
[Ad] Endereço:Center for Biomolecular Sciences, University of Illinois, Chicago, IL 60607, USA.
[Ti] Título:Co-produced natural ketolides methymycin and pikromycin inhibit bacterial growth by preventing synthesis of a limited number of proteins.
[So] Source:Nucleic Acids Res;45(16):9573-9582, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Antibiotics methymycin (MTM) and pikromycin (PKM), co-produced by Streptomyces venezuelae, represent minimalist macrolide protein synthesis inhibitors. Unlike other macrolides, which carry several side chains, a single desosamine sugar is attached to the macrolactone ring of MTM and PKM. In addition, the macrolactone scaffold of MTM is smaller than in other macrolides. The unusual structure of MTM and PKM and their simultaneous secretion by S. venezuelae bring about the possibility that two compounds would bind to distinct ribosomal sites. However, by combining genetic, biochemical and crystallographic studies, we demonstrate that MTM and PKM inhibit translation by binding to overlapping sites in the ribosomal exit tunnel. Strikingly, while MTM and PKM readily arrest the growth of bacteria, ∼40% of cellular proteins continue to be synthesized even at saturating concentrations of the drugs. Gel electrophoretic analysis shows that compared to other ribosomal antibiotics, MTM and PKM prevent synthesis of a smaller number of cellular polypeptides illustrating a unique mode of action of these antibiotics.
[Mh] Termos MeSH primário: Proteínas de Bactérias/biossíntese
Escherichia coli/efeitos dos fármacos
Macrolídeos/farmacologia
Inibidores da Síntese de Proteínas/farmacologia
[Mh] Termos MeSH secundário: Ligação Competitiva
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Macrolídeos/química
Macrolídeos/metabolismo
Fator G para Elongação de Peptídeos/genética
Ribossomos/química
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Macrolides); 0 (Peptide Elongation Factor G); 0 (Protein Synthesis Inhibitors); 16QGD97DXG (methymycin); FBM8G3Z439 (picromycin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx673


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[PMID]:28542628
[Au] Autor:Iwakura N; Yokoyama T; Quaglia F; Mitsuoka K; Mio K; Shigematsu H; Shirouzu M; Kaji A; Kaji H
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania, United States of America.
[Ti] Título:Chemical and structural characterization of a model Post-Termination Complex (PoTC) for the ribosome recycling reaction: Evidence for the release of the mRNA by RRF and EF-G.
[So] Source:PLoS One;12(5):e0177972, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A model Post-Termination Complex (PoTC) used for the discovery of Ribosome Recycling Factor (RRF) was purified and characterized by cryo-electron microscopic analysis and biochemical methods. We established that the model PoTC has mostly one tRNA, at the P/E or P/P position, together with one mRNA. The structural studies were supported by the biochemical measurement of bound tRNA and mRNA. Using this substrate, we establish that the release of tRNA, release of mRNA and splitting of ribosomal subunits occur during the recycling reaction. Order of these events is tRNA release first followed by mRNA release and splitting almost simultaneously. Moreover, we demonstrate that IF3 is not involved in any of the recycling reactions but simply prevents the re-association of split ribosomal subunits. Our finding demonstrates that the important function of RRF includes the release of mRNA, which is often missed by the use of a short ORF with the Shine-Dalgarno sequence near the termination site.
[Mh] Termos MeSH primário: Escherichia coli/genética
Escherichia coli/metabolismo
Terminação Traducional da Cadeia Peptídica/genética
Fator G para Elongação de Peptídeos/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Microscopia Crioeletrônica
Fator de Iniciação 3 em Procariotos/metabolismo
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Peptide Termination Factors); 0 (Prokaryotic Initiation Factor-3); 0 (RNA, Messenger); 0 (Ribosomal Proteins); 0 (ribosome releasing factor); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177972


  5 / 567 MEDLINE  
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[PMID]:28474852
[Au] Autor:Liu K; Rehfus JE; Mattson E; Kaiser CM
[Ad] Endereço:Department of Biology, Johns Hopkins University, Baltimore, Maryland.
[Ti] Título:The ribosome destabilizes native and non-native structures in a nascent multidomain protein.
[So] Source:Protein Sci;26(7):1439-1451, 2017 Jul.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Correct folding is a prerequisite for the biological activity of most proteins. Folding has largely been studied using in vitro refolding assays with isolated small, robustly folding proteins. A substantial fraction of all cellular proteomes is composed of multidomain proteins that are often not amenable to this approach, and their folding remains poorly understood. These large proteins likely begin to fold during their synthesis by the ribosome, a large molecular machine that translates the genetic code. The ribosome affects how folding proceeds, but the underlying mechanisms remain largely obscure. We have utilized optical tweezers to study the folding of elongation factor G, a multidomain protein composed of five domains. We find that interactions among unfolded domains interfere with productive folding in the full-length protein. The N-terminal G-domain constitutes an independently folding unit that, upon in vitro refolding, adopts two similar states that correspond to the natively folded and a non-native, possibly misfolded structure. The ribosome destabilizes both of these states, suggesting a mechanism by which terminal misfolding into highly stable, non-native structures is avoided. The ribosome may thus directly contribute to efficient folding by modulating the folding of nascent multidomain proteins.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Fator G para Elongação de Peptídeos/metabolismo
Biossíntese de Proteínas/fisiologia
Dobramento de Proteína
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Escherichia coli/química
Escherichia coli/genética
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Fator G para Elongação de Peptídeos/química
Fator G para Elongação de Peptídeos/genética
Domínios Proteicos
Ribossomos/química
Ribossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Peptide Elongation Factor G)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3189


  6 / 567 MEDLINE  
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[PMID]:28437082
[Au] Autor:Tsai TW; Yang H; Yin H; Xu S; Wang Y
[Ad] Endereço:Department of Biology and Biochemistry, ‡Department of Chemistry, University of Houston , Houston, Texas 77204, United States.
[Ti] Título:High-Efficiency "-1" and "-2" Ribosomal Frameshiftings Revealed by Force Spectroscopy.
[So] Source:ACS Chem Biol;12(6):1629-1635, 2017 Jun 16.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ribosomal frameshifting is a rare but ubiquitous process that is being studied extensively. Meanwhile, frameshifting motifs without any secondary mRNA structures were identified but rarely studied experimentally. We report unambiguous observation of highly efficient "-1" and "-2" frameshiftings on a GA G slippery mRNA without the downstream secondary structure, using force-induced remnant magnetization spectroscopy combined with unique probing schemes. The result represents the first experimental evidence of multiple frameshifting steps. It is also one of the rare reports of the "-2" frameshifting. Our assay removed the ambiguity of transcriptional slippage involvement in other frameshifting assays. Two significant insights for the frameshifting mechanism were revealed. First, EF-G·GTP is indispensable to frameshifting. Although EFG·GDPCP has been shown to prompt translocation before, we found that it could not induce frameshifting. This implies that the GTP hydrolysis is responsible for the codon-anticodon re-pairing in frameshifting, which corroborates our previous mechanical force measurement of EF-G·GTP. Second, translation in all three reading frames of the slippery sequence can be induced by the corresponding in-frame aminoacyl tRNAs. Although A-site tRNA is known to affect the partition between "0" and "-1" frameshifting, it has not been reported that all three reading frames can be translated by their corresponding tRNAs. The in vitro results were confirmed by toe-printing assay and protein sequencing.
[Mh] Termos MeSH primário: Mudança da Fase de Leitura do Gene Ribossômico
Análise Espectral/métodos
[Mh] Termos MeSH secundário: Sequência de Bases
Guanosina Trifosfato/metabolismo
Fator G para Elongação de Peptídeos
RNA Mensageiro
RNA de Transferência
Aminoacil-RNA de Transferência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (RNA, Messenger); 0 (RNA, Transfer, Amino Acyl); 86-01-1 (Guanosine Triphosphate); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00028


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[PMID]:28400018
[Au] Autor:Akineden Ö; Heinrich V; Gross M; Usleber E
[Ad] Endereço:Chair of Dairy Science, Institute of Veterinary Food Science, Justus-Liebig University Giessen, Ludwigstrasse 21, D-35390, Giessen, Germany. Electronic address: Oemer.Akineden@vetmed.uni-giessen.de.
[Ti] Título:Reassessment of Cronobacter spp. originally isolated as Enterobacter sakazakii from infant food.
[So] Source:Food Microbiol;65:44-50, 2017 Aug.
[Is] ISSN:1095-9998
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cronobacter spp. cause infant disease, several cases have been associated with powdered infant formulae (PIF). In the early 2000s, contamination of German PIF with these opportunistic pathogens was quite common. Before 2008, all isolates Cronobacter spp. had been classified as Enterobacter sakazakii, therefore little is known about species diversity within such isolates. Genetic, serologic, and biochemical traits of 80 Cronobacter isolates, originally obtained 2003-2006 within infant food surveys in Germany, were reassessed in this study. By sequencing of the fusA gene, all isolates were unambiguously assigned to two species, C. sakazakii (n = 73) and C. malonaticus (n = 7). PCR serotyping identified five C. sakazakii serotypes and two C. malonaticus serotypes, biochemical profiling yielded five biogroups. PFGE analysis also showed high heterogeneity in both species. Multilocus sequence typing of 26 selected isolates yielded 16 different sequence types (ST), including C. sakazakii ST 1 (n = 6) and the highly virulent ST 4 (n = 2). The results suggest that just two, but highly heterogeneous species were responsible for the Cronobacter contamination problem which challenged the German PIF industry in the beginning of this century. This fact may have influenced the success of efforts to identify and eliminate sources of contamination.
[Mh] Termos MeSH primário: Cronobacter sakazakii/isolamento & purificação
Cronobacter/classificação
Cronobacter/genética
Microbiologia de Alimentos
Fórmulas Infantis/microbiologia
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Cronobacter/isolamento & purificação
Cronobacter sakazakii/classificação
Cronobacter sakazakii/genética
Genótipo
Alemanha
Seres Humanos
Lactente
Tipagem de Sequências Multilocus
Fator G para Elongação de Peptídeos/genética
Reação em Cadeia da Polimerase
Estudos Retrospectivos
Sorotipagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170427
[Lr] Data última revisão:
170427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE


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[PMID]:28361860
[Au] Autor:Kashuba E; Mushtaq M
[Ad] Endereço:R.E. Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, NAS of Ukraine, Kyiv 03022, Ukraine.
[Ti] Título:Do MRPS18-2 and RB proteins cooperate to control cell stemness and differentiation, preventing cancer development?
[So] Source:Exp Oncol;39(1):12-16, 2017 Mar.
[Is] ISSN:1812-9269
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:In childhood tumors, including retinoblastoma, osteosarcoma, and neuroblastoma, the RB-E2F1 pathway is inactivated, as a rule. These tumors arise from precursor cells that fail to undergo the terminal differentiation. Noteworthy, the RB1-encoded protein (RB) does not control the cell cycle in embryonic stem cells. It has not been yet well understood how RB controls cell stemness and differentiation. The question arises why "inactive" RB is required for the survival and stemness of cells? Recently, we have found that overexpression of the RB-binding protein MRPS18-2 (S18-2) in primary fibroblasts leads to their immortalization, which is accompanied by the induction of embryonic stem cell markers and, eventually, malignant transformation. We suggest that cell stemness may be associated with high expression levels of both proteins, RB and S18-2. There must be a strict regulation of the expression levels of S18-2 and RB during embryogenesis. Disturbances in the expression of these proteins would lead to the abnormalities in development. We think that the S18-2 protein, together with the RB, plays a crucial role in the control on cell stemness and differentiation. We hope to uncover the new mechanisms of the cell fate determination. The S18-2 may serve as a new target for anticancer medicines, which will help to improve human health.
[Mh] Termos MeSH primário: Diferenciação Celular
Transformação Celular Neoplásica/metabolismo
Proteínas Mitocondriais/metabolismo
Proteína do Retinoblastoma/metabolismo
Proteínas Ribossômicas/metabolismo
Células-Tronco/metabolismo
[Mh] Termos MeSH secundário: Criança
Seres Humanos
Modelos Biológicos
Neuroblastoma/metabolismo
Neuroblastoma/patologia
Osteossarcoma/metabolismo
Osteossarcoma/patologia
Fator G para Elongação de Peptídeos/metabolismo
Retinoblastoma/metabolismo
Retinoblastoma/patologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GFM1 protein, human); 0 (Mitochondrial Proteins); 0 (Peptide Elongation Factor G); 0 (Retinoblastoma Protein); 0 (Ribosomal Proteins); 0 (ribosomal protein S18)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


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[PMID]:28342293
[Au] Autor:Carlson MA; Haddad BG; Weis AJ; Blackwood CS; Shelton CD; Wuerth ME; Walter JD; Spiegel PC
[Ad] Endereço:Department of Chemistry, Western Washington University, Bellingham, WA, USA.
[Ti] Título:Ribosomal protein L7/L12 is required for GTPase translation factors EF-G, RF3, and IF2 to bind in their GTP state to 70S ribosomes.
[So] Source:FEBS J;284(11):1631-1643, 2017 Jun.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribosomal protein L7/L12 is associated with translation initiation, elongation, and termination by the 70S ribosome. The guanosine 5' triphosphate hydrolase (GTPase) activity of elongation factor G (EF-G) requires the presence of L7/L12, which is critical for ribosomal translocation. Here, we have developed new methods for the complete depletion of L7/L12 from Escherichia coli 70S ribosomes to analyze the effect of L7/L12 on the activities of the GTPase factors EF-G, RF3, IF2, and LepA. Upon removal of L7/L12 from ribosomes, the GTPase activities of EF-G, RF3, and IF2 decreased to basal levels, while the activity of LepA decreased marginally. Upon reconstitution of ribosomes with recombinant L12, the GTPase activities of all GTPases returned to full activity. Moreover, ribosome binding assays indicated that EF-G, RF3, and IF2 require L7/L12 for stable binding in the GTP state, and LepA retained > 50% binding. Lastly, an EF-G∆G' truncation mutant possessed ribosome-dependent GTPase activity, which was insensitive to L7/L12. Our results indicate that L7/L12 is required for stable binding of ribosome-dependent GTPases that harbor direct interactions to the L7/L12 C-terminal domains, either through a G' domain (EF-G, RF3) or a unique N-terminal domain (IF2). Furthermore, we hypothesize this interaction is concomitant with counterclockwise ribosomal intersubunit rotation, which is required for translocation, initiation, and post-termination.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Proteínas de Escherichia coli/fisiologia
Guanosina Trifosfato/metabolismo
Fator G para Elongação de Peptídeos/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
Fator de Iniciação 2 em Procariotos/metabolismo
Proteínas Ribossômicas/fisiologia
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Ativação Enzimática
Proteínas de Escherichia coli/genética
Hidrólise
Mutagênese Sítio-Dirigida
Fatores de Iniciação de Peptídeos/metabolismo
Proteínas Recombinantes/metabolismo
Proteínas Ribossômicas/deficiência
Proteínas Ribossômicas/genética
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (LepA protein, E coli); 0 (Peptide Elongation Factor G); 0 (Peptide Initiation Factors); 0 (Peptide Termination Factors); 0 (Prokaryotic Initiation Factor-2); 0 (Recombinant Proteins); 0 (Ribosomal Proteins); 0 (prfC protein, E coli); 0 (rplL protein, E coli); 86-01-1 (Guanosine Triphosphate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14067


  10 / 567 MEDLINE  
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[PMID]:28099529
[Au] Autor:Das D; Samanta D; Bhattacharya A; Basu A; Das A; Ghosh J; Chakrabarti A; Das Gupta C
[Ad] Endereço:Department of Biophysics, Molecular Biology and Bioinformatics, University College of Science, University of Calcutta, Kolkata, India.
[Ti] Título:A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling.
[So] Source:PLoS One;12(1):e0170333, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Each cycle of translation initiation in bacterial cell requires free 50S and 30S ribosomal subunits originating from the post-translational dissociation of 70S ribosome from the previous cycle. Literature shows stable dissociation of 70S from model post-termination complexes by the concerted action of Ribosome Recycling Factor (RRF) and Elongation Factor G (EF-G) that interact with the rRNA bridge B2a/B2b joining 50S to 30S. In such experimental models, the role of full-length nascent protein was never considered seriously. We observed relatively slow release of full-length nascent protein from 50Sof post translation ribosome, and in that process, its toe prints on the rRNA in vivo and in in vitro translation with E.coli S30 extract. We reported earlier that a number of chemically unfolded proteins like bovine carbonic anhydrase (BCA), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), lysozyme, ovalbumin etc., when added to free 70Sin lieu of the full length nascent proteins, also interact with identical RNA regions of the 23S rRNA. Interestingly the rRNA nucleotides that slow down release of the C-terminus of full-length unfolded protein were found in close proximity to the B2a/B2b bridge. It indicated a potentially important chemical reaction conserved throughout the evolution. Here we set out to probe that conserved role of unfolded protein conformation in splitting the free or post-termination 70S. How both the RRF-EFG dependent and the plausible nascent protein-EFG dependent ribosome recycling pathways might be relevant in bacteria is discussed here.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Iniciação Traducional da Cadeia Peptídica/fisiologia
Terminação Traducional da Cadeia Peptídica/fisiologia
Biossíntese de Proteínas/fisiologia
Subunidades Ribossômicas Maiores de Bactérias/metabolismo
Subunidades Ribossômicas Menores de Bactérias/metabolismo
[Mh] Termos MeSH secundário: Animais
Anidrases Carbônicas/metabolismo
Bovinos
Embrião de Galinha
Escherichia coli/genética
L-Lactato Desidrogenase/metabolismo
Malato Desidrogenase/metabolismo
Muramidase/metabolismo
Ovalbumina/metabolismo
Fator G para Elongação de Peptídeos/metabolismo
Dobramento de Proteína
Proteínas Ribossômicas/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Ribosomal Proteins); 0 (ribosome releasing factor); 9006-59-1 (Ovalbumin); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 1.1.1.37 (Malate Dehydrogenase); EC 3.2.1.17 (Muramidase); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170333



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