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Pesquisa : D12.776.835.725.934 [Categoria DeCS]
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[PMID]:27986852
[Au] Autor:López-Alonso JP; Fabbretti A; Kaminishi T; Iturrioz I; Brandi L; Gil-Carton D; Gualerzi CO; Fucini P; Connell SR
[Ad] Endereço:Structural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
[Ti] Título:Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways.
[So] Source:Nucleic Acids Res;45(4):2179-2187, 2017 Feb 28.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In bacteria, the start site and the reading frame of the messenger RNA are selected by the small ribosomal subunit (30S) when the start codon, typically an AUG, is decoded in the P-site by the initiator tRNA in a process guided and controlled by three initiation factors. This process can be efficiently inhibited by GE81112, a natural tetrapeptide antibiotic that is highly specific toward bacteria. Here GE81112 was used to stabilize the 30S pre-initiation complex and obtain its structure by cryo-electron microscopy. The results obtained reveal the occurrence of changes in both the ribosome conformation and initiator tRNA position that may play a critical role in controlling translational fidelity. Furthermore, the structure highlights similarities with the early steps of initiation in eukaryotes suggesting that shared structural features guide initiation in all kingdoms of life.
[Mh] Termos MeSH primário: Iniciação Traducional da Cadeia Peptídica
RNA Mensageiro/genética
RNA de Transferência de Metionina/genética
Subunidades Ribossômicas Menores de Bactérias/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Escherichia coli/genética
Escherichia coli/metabolismo
Células Eucarióticas/metabolismo
Modelos Moleculares
Conformação Molecular
Fatores de Iniciação em Procariotos/química
Fatores de Iniciação em Procariotos/metabolismo
Biossíntese de Proteínas/genética
RNA Mensageiro/química
RNA Mensageiro/metabolismo
RNA de Transferência de Metionina/química
RNA de Transferência de Metionina/metabolismo
Subunidades Ribossômicas Maiores de Bactérias/química
Subunidades Ribossômicas Maiores de Bactérias/metabolismo
Subunidades Ribossômicas Menores de Bactérias/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prokaryotic Initiation Factors); 0 (RNA, Messenger); 0 (RNA, Transfer, Met)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1251


  2 / 39 MEDLINE  
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[PMID]:27784646
[Au] Autor:Kim DH; Kang SJ; Lee KY; Jang SB; Kang SM; Lee BJ
[Ad] Endereço:The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Republic of Korea.
[Ti] Título:Structure and dynamics study of translation initiation factor 1 from Staphylococcus aureus suggests its RNA binding mode.
[So] Source:Biochim Biophys Acta;1865(1):65-75, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Translation initiation, the rate-limiting step in the protein synthesis, is tightly regulated. As one of the translation initiation factors, translation initiation factor 1 (IF1) plays crucial roles not only in translation but also in many cellular processes that are important for genomic stability, such as the activity of RNA chaperones. Here, we characterize the RNA interactions and dynamics of IF1 from Staphylococcus aureus Mu50 (IF1 ) by NMR spectroscopy. First, the NMR-derived solution structure of IF1 revealed that IF1 adopts an oligonucleotide/oligosaccharide binding (OB)-fold. Structural comparisons showed large deviations in the α-helix and the following loop, which are potential RNA-binding regions of the OB-fold, as well as differences in the electrostatic potential surface among bacterial IF1s. Second, the N NMR relaxation data for IF1 indicated the flexible nature of the α-helix and the following loop region of IF1 . Third, RNA-binding properties were studied using FP assays and NMR titrations. FP binding assays revealed that IF1 binds to RNAs with moderate affinity. In combination with the structural analysis, the NMR titration results revealed the RNA binding sites. Taken together, these results show that IF1 binds RNAs with moderate binding affinity via the residues that occupy the large surface area of its ß-barrel. These findings suggest that IF1 is likely to bind RNA in various conformations rather than only at a specific site and indicate that the flexible RNA binding mode of IF1 is necessary for its interaction with various RNA substrates.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Fatores de Iniciação em Procariotos/química
Proteínas de Ligação a RNA/química
Staphylococcus aureus/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/ultraestrutura
Sítios de Ligação
Espectroscopia de Ressonância Magnética
Ressonância Magnética Nuclear Biomolecular
Iniciação Traducional da Cadeia Peptídica
Fatores de Iniciação em Procariotos/genética
Fatores de Iniciação em Procariotos/ultraestrutura
Ligação Proteica
Estrutura Secundária de Proteína
RNA Bacteriano/química
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/ultraestrutura
Alinhamento de Sequência
Staphylococcus aureus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Prokaryotic Initiation Factors); 0 (RNA, Bacterial); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161031
[St] Status:MEDLINE


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[PMID]:26983940
[Au] Autor:Bernal A; Hu Y; Palmer SO; Silva A; Bullard J; Zhang Y
[Ad] Endereço:Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.
[Ti] Título:(1)H, (13)C and (15)N resonance assignments and secondary structure analysis of translation initiation factor 1 from Pseudomonas aeruginosa.
[So] Source:Biomol NMR Assign;10(2):249-52, 2016 Oct.
[Is] ISSN:1874-270X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen and a primary cause of infection in humans. P. aeruginosa can acquire resistance against multiple groups of antimicrobial agents, including ß-lactams, aminoglycosides and fluoroquinolones, and multidrug resistance is increasing in this organism which makes treatment of the infections difficult and expensive. This has led to the unmet need for discovery of new compounds distinctly different from present antimicrobials. Protein synthesis is an essential metabolic process and a validated target for the development of new antibiotics. Translation initiation factor 1 from P. aeruginosa (Pa-IF1) is the smallest of the three initiation factors that acts to establish the 30S initiation complex to initiate translation during protein biosynthesis, and its structure is unknown. Here we report the (1)H, (13)C and (15)N chemical shift assignments of Pa-IF1 as the basis for NMR structure determination and interaction studies. Secondary structure analyses deduced from the NMR chemical shift data have identified five ß-strands with an unusually extended ß-strand at the C-terminal end of the protein and one short α-helix arranged in the sequential order ß1-ß2-ß3-α1-ß4-ß5. This is further supported by (15)N-{(1)H} hetero NOEs. These secondary structure elements suggest the Pa-IF1 adopts the typical ß-barrel structure and is composed of an oligomer-binding motif.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Ressonância Magnética Nuclear Biomolecular
Fatores de Iniciação em Procariotos/química
Pseudomonas aeruginosa
[Mh] Termos MeSH secundário: Estrutura Secundária de Proteína
Pseudomonas aeruginosa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Prokaryotic Initiation Factors)
[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:160318
[St] Status:MEDLINE
[do] DOI:10.1007/s12104-016-9678-7


  4 / 39 MEDLINE  
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[PMID]:25996652
[Au] Autor:Calligari PA; Calandrini V; Ollivier J; Artero JB; Härtlein M; Johnson M; Kneller GR
[Ad] Endereço:†SISSA, International School for Advanced Studies, via Bonomea 265, 34136 Trieste, Italy.
[Ti] Título:Adaptation of Extremophilic Proteins with Temperature and Pressure: Evidence from Initiation Factor 6.
[So] Source:J Phys Chem B;119(25):7860-73, 2015 Jun 25.
[Is] ISSN:1520-5207
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, we study dynamical properties of an extremophilic protein, Initiation Factor 6 (IF6), produced by the archeabacterium Methanocaldococcus jannascii, which thrives close to deep-sea hydrothermal vents where temperatures reach 80 °C and the pressure is up to 750 bar. Molecular dynamics simulations (MD) and quasi-elastic neutron scattering (QENS) measurements give new insights into the dynamical properties of this protein with respect to its eukaryotic and mesophilic homologue. Results obtained by MD are supported by QENS data and are interpreted within the framework of a fractional Brownian dynamics model for the characterization of protein relaxation dynamics. IF6 from M. jannaschii at high temperature and pressure shares similar flexibility with its eukaryotic homologue from S. cerevisieae under ambient conditions. This work shows for the first time, to our knowledge, that the very common pattern of corresponding states for thermophilic protein adaptation can be extended to thermo-barophilic proteins. A detailed analysis of dynamic properties and of local structural fluctuations reveals a complex pattern for "corresponding" structural flexibilities. In particular, in the case of IF6, the latter seems to be strongly related to the entropic contribution given by an additional, C-terminal, 20 amino-acid tail which is evolutionary conserved in all mesophilic IF6s.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Fatores de Iniciação em Procariotos/química
[Mh] Termos MeSH secundário: Hidrodinâmica
Methanocaldococcus
Simulação de Dinâmica Molecular
Difração de Nêutrons
Maleabilidade
Pressão
Proteínas de Saccharomyces cerevisiae/química
Temperatura Ambiente
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Prokaryotic Initiation Factors); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150625
[Lr] Data última revisão:
150625
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150522
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jpcb.5b02034


  5 / 39 MEDLINE  
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[PMID]:25378333
[Au] Autor:Balakrishnan R; Oman K; Shoji S; Bundschuh R; Fredrick K
[Ad] Endereço:Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
[Ti] Título:The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli.
[So] Source:Nucleic Acids Res;42(21):13370-83, 2014 Dec 01.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:LepA is a paralog of EF-G found in all bacteria. Deletion of lepA confers no obvious growth defect in Escherichia coli, and the physiological role of LepA remains unknown. Here, we identify nine strains (ΔdksA, ΔmolR1, ΔrsgA, ΔtatB, ΔtonB, ΔtolR, ΔubiF, ΔubiG or ΔubiH) in which ΔlepA confers a synthetic growth phenotype. These strains are compromised for gene regulation, ribosome assembly, transport and/or respiration, indicating that LepA contributes to these functions in some way. We also use ribosome profiling to deduce the effects of LepA on translation. We find that loss of LepA alters the average ribosome density (ARD) for hundreds of mRNA coding regions in the cell, substantially reducing ARD in many cases. By contrast, only subtle and codon-specific changes in ribosome distribution along mRNA are seen. These data suggest that LepA contributes mainly to the initiation phase of translation. Consistent with this interpretation, the effect of LepA on ARD is related to the sequence of the Shine-Dalgarno region. Global perturbation of gene expression in the ΔlepA mutant likely explains most of its phenotypes.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/fisiologia
Escherichia coli/genética
Iniciação Traducional da Cadeia Peptídica
Fatores de Iniciação de Peptídeos/fisiologia
Fatores de Iniciação em Procariotos/fisiologia
[Mh] Termos MeSH secundário: Domínio Catalítico
Escherichia coli/enzimologia
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Deleção de Genes
Elongação Traducional da Cadeia Peptídica
Fatores de Iniciação de Peptídeos/química
Fatores de Iniciação de Peptídeos/genética
Fatores de Iniciação de Peptídeos/metabolismo
Fenótipo
Fatores de Iniciação em Procariotos/química
Fatores de Iniciação em Procariotos/genética
Fatores de Iniciação em Procariotos/metabolismo
Estrutura Terciária de Proteína
RNA Mensageiro/análise
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (LepA protein, E coli); 0 (Peptide Initiation Factors); 0 (Prokaryotic Initiation Factors); 0 (RNA, Messenger); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141108
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gku1098


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[PMID]:24271401
[Au] Autor:Märtens B; Manoharadas S; Hasenöhrl D; Zeichen L; Bläsi U
[Ad] Endereço:Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, Center of Molecular Biology, University of Vienna, Dr. Bohrgasse 9, 1030 Vienna, Austria.
[Ti] Título:Back to translation: removal of aIF2 from the 5'-end of mRNAs by translation recovery factor in the crenarchaeon Sulfolobus solfataricus.
[So] Source:Nucleic Acids Res;42(4):2505-11, 2014 Feb.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The translation initiation factor aIF2 of the crenarchaeon Sulfolobus solfataricus (Sso) recruits initiator tRNA to the ribosome and stabilizes mRNAs by binding via the γ-subunit to their 5'-triphosphate end. It has been hypothesized that the latter occurs predominantly during unfavorable growth conditions, and that aIF2 or aIF2-γ is released on relief of nutrient stress to enable in particular anew translation of leaderless mRNAs. As leaderless mRNAs are prevalent in Sso and aIF2-γ bound to the 5'-end of a leaderless RNA inhibited ribosome binding in vitro, we aimed at elucidating the mechanism underlying aIF2/aIF2-γ recycling from mRNAs. We have identified a protein termed Trf (translation recovery factor) that co-purified with trimeric aIF2 during outgrowth of cells from prolonged stationary phase. Subsequent in vitro studies revealed that Trf triggers the release of trimeric aIF2 from RNA, and that Trf directly interacts with the aIF2-γ subunit. The importance of Trf is further underscored by an impaired protein synthesis during outgrowth from stationary phase in a Sso trf deletion mutant.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Iniciação Traducional da Cadeia Peptídica
Fatores de Iniciação em Procariotos/metabolismo
RNA Mensageiro/metabolismo
Sulfolobus solfataricus/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Proteínas Arqueais/isolamento & purificação
Mutação
Fatores de Iniciação em Procariotos/isolamento & purificação
Sulfolobus solfataricus/crescimento & desenvolvimento
Sulfolobus solfataricus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Prokaryotic Initiation Factors); 0 (RNA, Messenger)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131126
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkt1169


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[PMID]:24358293
[Au] Autor:Flåtten I; Skarstad K
[Ad] Endereço:Department of Cell Biology, Institute for Cancer Research, The Norwegian Radiumhospital, Oslo University Hospital, Oslo, Norway.
[Ti] Título:The Fis protein has a stimulating role in initiation of replication in Escherichia coli in vivo.
[So] Source:PLoS One;8(12):e83562, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Fis protein is a nucleoid associated protein that has previously been reported to act negatively in initiation of replication in Escherichia coli. In this work we have examined the influence of this protein on the initiation of replication under different growth conditions using flow cytometry. The Fis protein was found to be increasingly important with increasing growth rate. During multi-fork replication severe under-initiation occurred in cells lacking the Fis protein; the cells initiated at an elevated mass, had fewer origins per cell and the origins were not initiated in synchrony. These results suggest a positive role for the Fis protein in the initiation of replication.
[Mh] Termos MeSH primário: Replicação do DNA/genética
Proteínas de Escherichia coli/fisiologia
Escherichia coli/genética
Fator Proteico para Inversão de Estimulação/fisiologia
[Mh] Termos MeSH secundário: Cromossomos Bacterianos/genética
Cromossomos Bacterianos/metabolismo
DNA Bacteriano/genética
Escherichia coli/crescimento & desenvolvimento
Organismos Geneticamente Modificados
Fatores de Iniciação em Procariotos/fisiologia
Iniciação da Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (Factor For Inversion Stimulation Protein); 0 (Fis protein, E coli); 0 (Prokaryotic Initiation Factors)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0083562


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[PMID]:24244275
[Au] Autor:Gäbel K; Schmitt J; Schulz S; Näther DJ; Soppa J
[Ad] Endereço:Institute for Molecular Biosciences, Biocentre, Goethe-University, Frankfurt, Germany.
[Ti] Título:A comprehensive analysis of the importance of translation initiation factors for Haloferax volcanii applying deletion and conditional depletion mutants.
[So] Source:PLoS One;8(11):e77188, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translation is an important step in gene expression. The initiation of translation is phylogenetically diverse, since currently five different initiation mechanisms are known. For bacteria the three initiation factors IF1 - IF3 are described in contrast to archaea and eukaryotes, which contain a considerably higher number of initiation factor genes. As eukaryotes and archaea use a non-overlapping set of initiation mechanisms, orthologous proteins of both domains do not necessarily fulfill the same function. The genome of Haloferax volcanii contains 14 annotated genes that encode (subunits of) initiation factors. To gain a comprehensive overview of the importance of these genes, it was attempted to construct single gene deletion mutants of all genes. In 9 cases single deletion mutants were successfully constructed, showing that the respective genes are not essential. In contrast, the genes encoding initiation factors aIF1, aIF2γ, aIF5A, aIF5B, and aIF6 were found to be essential. Factors aIF1A and aIF2ß are encoded by two orthologous genes in H. volcanii. Attempts to generate double mutants failed in both cases, indicating that also these factors are essential. A translatome analysis of one of the single aIF2ß deletion mutants revealed that the translational efficiency of the second ortholog was enhanced tenfold and thus the two proteins can replace one another. The phenotypes of the single deletion mutants also revealed that the two aIF1As and aIF2ßs have redundant but not identical functions. Remarkably, the gene encoding aIF2α, a subunit of aIF2 involved in initiator tRNA binding, could be deleted. However, the mutant had a severe growth defect under all tested conditions. Conditional depletion mutants were generated for the five essential genes. The phenotypes of deletion mutants and conditional depletion mutants were compared to that of the wild-type under various conditions, and growth characteristics are discussed.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Deleção de Genes
Haloferax volcanii/genética
Iniciação Traducional da Cadeia Peptídica/fisiologia
Fatores de Iniciação em Procariotos/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Haloferax volcanii/metabolismo
Fatores de Iniciação em Procariotos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Prokaryotic Initiation Factors)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0077188


  9 / 39 MEDLINE  
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[PMID]:23474467
[Au] Autor:Mutalik VK; Guimaraes JC; Cambray G; Mai QA; Christoffersen MJ; Martin L; Yu A; Lam C; Rodriguez C; Bennett G; Keasling JD; Endy D; Arkin AP
[Ad] Endereço:BIOFAB International Open Facility Advancing Biotechnology, Emeryville, California, USA.
[Ti] Título:Quantitative estimation of activity and quality for collections of functional genetic elements.
[So] Source:Nat Methods;10(4):347-53, 2013 Apr.
[Is] ISSN:1548-7105
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The practice of engineering biology now depends on the ad hoc reuse of genetic elements whose precise activities vary across changing contexts. Methods are lacking for researchers to affordably coordinate the quantification and analysis of part performance across varied environments, as needed to identify, evaluate and improve problematic part types. We developed an easy-to-use analysis of variance (ANOVA) framework for quantifying the performance of genetic elements. For proof of concept, we assembled and analyzed combinations of prokaryotic transcription and translation initiation elements in Escherichia coli. We determined how estimation of part activity relates to the number of unique element combinations tested, and we show how to estimate expected ensemble-wide part activity from just one or two measurements. We propose a new statistic, biomolecular part 'quality', for tracking quantitative variation in part performance across changing contexts.
[Mh] Termos MeSH primário: Bioengenharia/métodos
Escherichia coli/metabolismo
Fatores de Iniciação de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica/fisiologia
Biblioteca Gênica
Iniciação Traducional da Cadeia Peptídica
Fatores de Iniciação em Procariotos/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Peptide Initiation Factors); 0 (Prokaryotic Initiation Factors)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130312
[St] Status:MEDLINE
[do] DOI:10.1038/nmeth.2403


  10 / 39 MEDLINE  
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[PMID]:23474465
[Au] Autor:Mutalik VK; Guimaraes JC; Cambray G; Lam C; Christoffersen MJ; Mai QA; Tran AB; Paull M; Keasling JD; Arkin AP; Endy D
[Ad] Endereço:BIOFAB International Open Facility Advancing Biotechnology, Emeryville, California, USA.
[Ti] Título:Precise and reliable gene expression via standard transcription and translation initiation elements.
[So] Source:Nat Methods;10(4):354-60, 2013 Apr.
[Is] ISSN:1548-7105
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An inability to reliably predict quantitative behaviors for novel combinations of genetic elements limits the rational engineering of biological systems. We developed an expression cassette architecture for genetic elements controlling transcription and translation initiation in Escherichia coli: transcription elements encode a common mRNA start, and translation elements use an overlapping genetic motif found in many natural systems. We engineered libraries of constitutive and repressor-regulated promoters along with translation initiation elements following these definitions. We measured activity distributions for each library and selected elements that collectively resulted in expression across a 1,000-fold observed dynamic range. We studied all combinations of curated elements, demonstrating that arbitrary genes are reliably expressed to within twofold relative target expression windows with ∼93% reliability. We expect the genetic element definitions validated here can be collectively expanded to create collections of public-domain standard biological parts that support reliable forward engineering of gene expression at genome scales.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Fatores de Iniciação em Procariotos/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica/fisiologia
Biblioteca Gênica
Engenharia Genética
Genoma Bacteriano
Fatores de Iniciação em Procariotos/genética
Regiões Promotoras Genéticas/genética
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Prokaryotic Initiation Factors); 0 (RNA, Bacterial); 0 (RNA, Messenger)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130312
[St] Status:MEDLINE
[do] DOI:10.1038/nmeth.2404



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