Base de dados : MEDLINE
Pesquisa : A11.284.430.214.190.875.811 [Categoria DeCS]
Referências encontradas : 28235 [refinar]
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[PMID]:29178822
[Au] Autor:Bowman MJ; Pulman JA; Liu TL; Childs KL
[Ad] Endereço:Department of Plant Biology, Michigan State University, 612 Wilson Rd, Room 166, East Lansing, MI, 48824, USA.
[Ti] Título:A modified GC-specific MAKER gene annotation method reveals improved and novel gene predictions of high and low GC content in Oryza sativa.
[So] Source:BMC Bioinformatics;18(1):522, 2017 Nov 25.
[Is] ISSN:1471-2105
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Accurate structural annotation depends on well-trained gene prediction programs. Training data for gene prediction programs are often chosen randomly from a subset of high-quality genes that ideally represent the variation found within a genome. One aspect of gene variation is GC content, which differs across species and is bimodal in grass genomes. When gene prediction programs are trained on a subset of grass genes with random GC content, they are effectively being trained on two classes of genes at once, and this can be expected to result in poor results when genes are predicted in new genome sequences. RESULTS: We find that gene prediction programs trained on grass genes with random GC content do not completely predict all grass genes with extreme GC content. We show that gene prediction programs that are trained with grass genes with high or low GC content can make both better and unique gene predictions compared to gene prediction programs that are trained on genes with random GC content. By separately training gene prediction programs with genes from multiple GC ranges and using the programs within the MAKER genome annotation pipeline, we were able to improve the annotation of the Oryza sativa genome compared to using the standard MAKER annotation protocol. Gene structure was improved in over 13% of genes, and 651 novel genes were predicted by the GC-specific MAKER protocol. CONCLUSIONS: We present a new GC-specific MAKER annotation protocol to predict new and improved gene models and assess the biological significance of this method in Oryza sativa. We expect that this protocol will also be beneficial for gene prediction in any organism with bimodal or other unusual gene GC content.
[Mh] Termos MeSH primário: Genoma de Planta
Anotação de Sequência Molecular/métodos
Oryza/genética
[Mh] Termos MeSH secundário: Composição de Bases
Cadeias de Markov
RNA de Plantas/química
RNA de Plantas/isolamento & purificação
RNA de Plantas/metabolismo
Ribossomos/metabolismo
Análise de Sequência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Plant)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1186/s12859-017-1942-z


  2 / 28235 MEDLINE  
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[PMID]:28470612
[Au] Autor:Berger I; Jiang Q; Schulze RJ; Collinson I; Schaffitzel C
[Ad] Endereço:The School of Biochemistry, University Walk, University of Bristol, Clifton, BS8 1TD, UK. imre.berger@bristol.ac.uk.
[Ti] Título:Multiprotein Complex Production in E. coli: The SecYEG-SecDFYajC-YidC Holotranslocon.
[So] Source:Methods Mol Biol;1586:279-290, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A modular approach for balanced overexpression of recombinant multiprotein complexes in E. coli is described, with the prokaryotic protein secretase/insertase complex, the SecYEG-SecDFYajC-YidC holotranslocon (HTL), used as an example. This procedure has been implemented here in the ACEMBL system. The protocol details the design principles of the monocistronic or polycistronic DNA constructs, the expression and purification of functional HTL and its association with translating ribosome nascent chain (RNC) complexes into a RNC-HTL supercomplex.
[Mh] Termos MeSH primário: Escherichia coli/genética
Complexos Multiproteicos/genética
Canais de Translocação SEC/genética
[Mh] Termos MeSH secundário: Clonagem Molecular/métodos
DNA Recombinante/genética
Proteínas de Escherichia coli/genética
Proteínas de Membrana Transportadoras/genética
Plasmídeos/genética
Proteínas Recombinantes/genética
Ribossomos/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Recombinant); 0 (Escherichia coli Proteins); 0 (Membrane Transport Proteins); 0 (Multiprotein Complexes); 0 (Recombinant Proteins); 0 (SEC Translocation Channels); 0 (SecD protein, E coli); 0 (YIDC protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_18


  3 / 28235 MEDLINE  
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[PMID]:28467675
[Au] Autor:Urakov VN; Mitkevich OV; Safenkova IV; Ter-Avanesyan MD
[Ad] Endereço:Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia.
[Ti] Título:Ribosome-bound Pub1 modulates stop codon decoding during translation termination in yeast.
[So] Source:FEBS J;284(12):1914-1930, 2017 06.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, termination of translation is controlled by polypeptide chain release factors eRF1 and eRF3, of which the former recognizes nonsense codons, while the latter interacts with eRF1 and stimulates polypeptide release from the ribosome in a GTP- dependent manner, and ABCE1, which facilitates ribosome recycling. In this work, we demonstrate that Pub1, a yeast protein known to be involved in stress granule formation, regulation of gene expression, and organization of the tubulin cytoskeleton, also plays a role in translation termination. Pub1 was shown to bind to ribosomes independent of eRF1 and eRF3 and to interact with the N-terminal glutamine-/asparagine-rich prion domain of eRF3 via its short C-terminal glutamine-rich tract. High velocity sedimentation in sucrose gradient demonstrated that Pub1 was preferentially associated with heavy polysomes enriched with terminating ribosomes. Lack of Pub1 decreased efficiency of nonsense readthrough at a majority but not all tetranucleotide stop signals. This distinguishes Pub1 from most other known binding partners of the release factors which were shown to modulate readthrough of all nonsense codons uniformly. The obtained data show that Pub1 can act as an accessory translation factor involved in fine-tuning of translation termination.
[Mh] Termos MeSH primário: Fatores de Terminação de Peptídeos/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Ribossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Códon de Terminação
Terminação Traducional da Cadeia Peptídica
Fatores de Terminação de Peptídeos/genética
Proteínas de Ligação a Poli(A)/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/genética
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Codon, Terminator); 0 (PUB1 protein, S cerevisiae); 0 (Peptide Termination Factors); 0 (Poly(A)-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (peptide-chain-release factor 3)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14099


  4 / 28235 MEDLINE  
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[PMID]:29274908
[Au] Autor:Luo C; Liu A; Long W; Liao H; Yang Y
[Ad] Endereço:Bamboo Diseases and Pests Control and Resources Development Key Laboratory of Sichuan Province, Leshan Normal University, Leshan 614000, Sichuan, China; College of Life Science, Leshan Normal University, Leshan 614000, Sichuan, China.
[Ti] Título:Transcriptome analysis of Cyrtotrachelus buqueti in two cities in China.
[So] Source:Gene;647:1-12, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In order to reduce the Cyrtotrachelus buqueti population, which is a serious pest in the bamboo industry, a range of approaches is required, which will be dependent on diverse gene expression influenced by environmental factors. In this study, samples from two regions of China, Muchuan in Sichuan Province and Chishui in Guizhou Province, were investigated through RNA-seq. Approximately 44 million high-quality reads were generated and 94.2% of the data was mapped to the transcriptome. A total of 15,641 out of the 29,406 identified genes were predicted. Moreover, 348 genes were differentially expressed between the two groups of imagoes (77 upregulated and 271 downregulated). The functional analysis showed that these genes were significantly enriched in the ribosome and metabolic pathway categories. The candidate genes contributing to the reduction in C. buqueti included 41 genes involved in the ribosome constitution category, five in the one­carbon pool pathway by folate category, and five heat shock protein genes. The downregulation of these candidate genes seems to have impaired metabolic processes, such as protein, DNA, RNA, and purine synthesis, as well as carbon and folate metabolism, subsequently resulting in the observed population reduction of C. buqueti. Furthermore, temperature, heavy metal content, and pH might influence the population by altering the expressions of genes involved in these metabolic processes.
[Mh] Termos MeSH primário: Transcriptoma/genética
Gorgulhos/genética
[Mh] Termos MeSH secundário: Animais
China
Cidades
Regulação para Baixo/genética
Perfilação da Expressão Gênica/métodos
Redes e Vias Metabólicas/genética
RNA/genética
Ribossomos/genética
Análise de Sequência de RNA/métodos
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
63231-63-0 (RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171225
[St] Status:MEDLINE


  5 / 28235 MEDLINE  
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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


  6 / 28235 MEDLINE  
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[PMID]:28743463
[Au] Autor:Rivas-Aravena A; Muñoz P; Jorquera P; Diaz A; Reinoso C; González-Catrilelbún S; Sandino AM
[Ad] Endereço:Comisión Chilena de Energía Nuclear, Departamento de Aplicaciones Nucleares, Laboratorio de Radiobiología Celular y Molecular. Nueva Bilbao 12501, Las Condes, Santiago, Chile; Universidad San Sebastián, Facultad de Ciencias, Lota 2465, Providencia, Santiago, Chile. Electronic address: andrea.rivas@c
[Ti] Título:Study of RNA-A Initiation Translation of The Infectious Pancreatic Necrosis Virus.
[So] Source:Virus Res;240:121-129, 2017 08 15.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The infectious pancreatic necrosis virus (IPNV) is a salmonid pathogen that causes significant economic losses to the aquaculture industry. IPNV is a non-enveloped virus containing two uncapped and non-polyadenylated double strand RNA genomic segments, RNA-A and RNA-B. The viral protein Vpg is covalently attached to the 5' end of both segments. There is little knowledge about its viral cycle, particularly about the translation of the RNAs. Through experiments using mono and bicistronic reporters, in this work we show that the 120-nucleotide-long 5'-UTR of RNA-A contains an internal ribosome entry site (IRES) that functions efficiently both in vitro and in salmon cells. IRES activity is strongly dependent on temperature. Also, the IRES structure is confined to the 5'UTR and is not affected by the viral coding sequence. This is the first report of IRES activity in a fish virus and can give us tools to generate antivirals to attack the virus without affecting fish directly.
[Mh] Termos MeSH primário: Infecções por Birnaviridae/veterinária
Doenças dos Peixes/virologia
Vírus da Necrose Pancreática Infecciosa/genética
Biossíntese de Proteínas
RNA Viral/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Animais
Infecções por Birnaviridae/virologia
Regulação Viral da Expressão Gênica
Vírus da Necrose Pancreática Infecciosa/química
Vírus da Necrose Pancreática Infecciosa/metabolismo
Sítios Internos de Entrada Ribossomal
Conformação de Ácido Nucleico
RNA Mensageiro/química
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Viral/química
RNA Viral/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Salmo salar
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Internal Ribosome Entry Sites); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


  7 / 28235 MEDLINE  
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[PMID]:29237735
[Au] Autor:Dougherty JD
[Ad] Endereço:Departments of Genetics and Psychiatry, Washington University School of Medicine, St. Louis, Missouri 63110 jdougherty@genetics.wustl.edu.
[Ti] Título:The Expanding Toolkit of Translating Ribosome Affinity Purification.
[So] Source:J Neurosci;37(50):12079-12087, 2017 Dec 13.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translating ribosome affinity purification is a method initially developed for profiling mRNA from genetically defined cell types in complex tissues. It has been applied both to identify target molecules in cell types that are important for controlling a variety of behaviors in the brain, and to understand the molecular consequences on those cells due to experimental manipulations, ranging from drugs of abuse to disease-causing mutations. Since its inception, a variety of methodological advances are opening new avenues of investigation. These advances include a variety of new methods for targeting cells for translating ribosome affinity purification by features such as their projections or activity, additional tags and mouse reagents increasing the flexibility of the system, and new modifications of the method specifically focused on studying the regulation of translation. The latter includes methods to assess cell type-specific regulation of translation in specific subcellular compartments. Here, I provide a summary of these recent advances and resources, highlighting both new experimental opportunities and areas for future technical development.
[Mh] Termos MeSH primário: Fracionamento Celular/métodos
Perfilação da Expressão Gênica/métodos
Ensaios de Triagem em Larga Escala/métodos
Separação Imunomagnética/métodos
Neuroglia/ultraestrutura
Neurônios/ultraestrutura
Biossíntese de Proteínas
Ribossomos
[Mh] Termos MeSH secundário: Marcadores de Afinidade
Animais
Encéfalo/citologia
Fracionamento Celular/tendências
Linhagem Celular
Cromossomos Artificiais Bacterianos
Dependovirus/genética
Eletroporação
Imunofluorescência
Previsões
Genes Reporter
Vetores Genéticos/genética
Proteínas de Fluorescência Verde/análise
Proteínas de Fluorescência Verde/genética
Camundongos
Neuroglia/metabolismo
Neurônios/classificação
Neurônios/metabolismo
Fases de Leitura Aberta/genética
RNA Mensageiro/genética
RNA Mensageiro/isolamento & purificação
Proteínas Recombinantes de Fusão/análise
Proteínas Ribossômicas/análise
Proteínas Ribossômicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Affinity Labels); 0 (RNA, Messenger); 0 (Recombinant Fusion Proteins); 0 (Ribosomal Proteins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1929-17.2017


  8 / 28235 MEDLINE  
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[PMID]:29247799
[Au] Autor:Varland S; Myklebust LM; Goksøyr SØ; Glomnes N; Torsvik J; Varhaug JE; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Thormøhlensgate 55, 5006 Bergen, Norway.
[Ti] Título:Identification of an alternatively spliced nuclear isoform of human N-terminal acetyltransferase Naa30.
[So] Source:Gene;644:27-37, 2018 Feb 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is a highly abundant and important protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs). In humans, six different NATs have been identified (NatA-NatF), each composed of individual subunits and acetylating a distinct set of substrates. Along with most NATs, NatC acts co-translationally at the ribosome. The NatC complex consists of the catalytic subunit Naa30 and the auxiliary subunits Naa35 and Naa38, and can potentially Nt-acetylate cytoplasmic proteins when the initiator methionine is followed by a bulky hydrophobic/amphipathic residue at position 2. Here, we have identified a splice variant of human NAA30, which encodes a truncated protein named Naa30 . The splice variant was abundantly present in thyroid cancer tissues and in several different human cancer cell lines. Surprisingly, Naa30 localized predominantly to the nucleus, as opposed to annotated Naa30 which has a cytoplasmic localization. Full-length Naa30 acetylated a classical NatC substrate peptide in vitro, whereas no significant NAT activity was detected for Naa30 Due to the nuclear localization, we also examined acetyltransferase activity towards lysine residues. Neither full-length Naa30 nor Naa30 displayed any lysine acetyltransferase activity. Overexpression of full-length Naa30 increased cell viability via inhibition of apoptosis. In contrast, Naa30 did not exert an anti-apoptotic effect. In sum, we identified a novel and widely expressed Naa30 isoform with a potential non-catalytic role in the nucleus.
[Mh] Termos MeSH primário: Núcleo Celular/genética
Acetiltransferase N-Terminal C/genética
Acetiltransferases N-Terminal/genética
Isoformas de Proteínas/genética
Processamento de RNA/genética
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Linhagem Celular
Linhagem Celular Tumoral
Sobrevivência Celular/genética
Células HEK293
Células HeLa
Seres Humanos
Lisina/genética
Células MCF-7
Processamento de Proteína Pós-Traducional/genética
Ribossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (N-Terminal Acetyltransferases); EC 2.3.1.88 (NAA30 protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


  9 / 28235 MEDLINE  
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[PMID]:28450575
[Au] Autor:Rowley JW; Weyrich AS
[Ad] Endereço:UNIVERSITY OF UTAH SCHOOL OF MEDICINE.
[Ti] Título:Ribosomes in platelets protect the messenger.
[So] Source:Blood;129(17):2343-2345, 2017 04 27.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Plaquetas
Ribossomos
[Mh] Termos MeSH secundário: Seres Humanos
Biossíntese de Proteínas
Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-03-770180


  10 / 28235 MEDLINE  
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[PMID]:28468753
[Au] Autor:Beckert B; Abdelshahid M; Schäfer H; Steinchen W; Arenz S; Berninghausen O; Beckmann R; Bange G; Turgay K; Wilson DN
[Ad] Endereço:Gene Center, Department for Biochemistry and Center for integrated Protein Science Munich (CiPSM), University of Munich, Munich, Germany.
[Ti] Título:Structure of the hibernating 100S ribosome reveals the basis for 70S dimerization.
[So] Source:EMBO J;36(14):2061-2072, 2017 07 14.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Under stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In , dimerization of 70S ribosomes into 100S requires the action of the ribosome modulation factor (RMF) and the hibernation-promoting factor (HPF). Most other bacteria lack RMF and instead contain a long form HPF (LHPF), which is necessary and sufficient for 100S formation. While some structural information exists as to how RMF and HPF mediate formation of 100S ( 100S), structural insight into 100S formation by LHPF has so far been lacking. Here we present a cryo-EM structure of the hibernating 100S ( 100S), revealing that the C-terminal domain (CTD) of the LHPF occupies a site on the 30S platform distinct from RMF Moreover, unlike RMF, the HPF-CTD is directly involved in forming the dimer interface, thereby illustrating the divergent mechanisms by which 100S formation is mediated in the majority of bacteria that contain LHPF, compared to some γ-proteobacteria, such as .
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Bacillus subtilis/ultraestrutura
Proteínas de Bactérias/metabolismo
Dimerização
Proteínas de Choque Térmico/metabolismo
Ribossomos/metabolismo
Ribossomos/ultraestrutura
[Mh] Termos MeSH secundário: Microscopia Crioeletrônica
Modelos Moleculares
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Heat-Shock Proteins); 0 (yvyD protein, Bacillus subtilis)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180106
[Lr] Data última revisão:
180106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201696189



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