Base de dados : MEDLINE
Pesquisa : G04.128 [Categoria DeCS]
Referências encontradas : 9712 [refinar]
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  1 / 9712 MEDLINE  
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[PMID]:28464535
[Au] Autor:Huttanus HM; Feng X
[Ad] Endereço:Biological Systems Engineering, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA.
[Ti] Título:Compartmentalized metabolic engineering for biochemical and biofuel production.
[So] Source:Biotechnol J;12(6), 2017 Jun.
[Is] ISSN:1860-7314
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Sub-cellular compartments create specialized reaction chambers in eukaryotes. These compartments provide favorable micro-environments for many metabolic processes. Recently, metabolic engineers have explored the concept of pathway compartmentalization to enhance the performance of metabolic pathways. This strategy offers many unique advantages, including (i) increased local concentrations of enzymes and substrates, (ii) accessing alternate substrate pools, (iii) separation from competing reactions, and (iv) isolation of harmful intermediates or conditions needed for the pathway. In this review, the method of localizing metabolic pathways into specific organelles as well as the benefits of pathway compartmentalization in terms of enhancing the production of value-added chemicals is discussed.
[Mh] Termos MeSH primário: Biocombustíveis
Engenharia Metabólica
Redes e Vias Metabólicas
[Mh] Termos MeSH secundário: Bactérias/metabolismo
Compartimento Celular
Cloroplastos/metabolismo
Mitocôndrias/metabolismo
Organelas/metabolismo
Peroxissomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biofuels)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/biot.201700052


  2 / 9712 MEDLINE  
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[PMID]:28743798
[Au] Autor:Chen W; Huang H; Hatori R; Kornberg TB
[Ad] Endereço:Cardiovascular Research Institute, University of California, San Francisco, CA 94143, USA.
[Ti] Título:Essential basal cytonemes take up Hedgehog in the wing imaginal disc.
[So] Source:Development;144(17):3134-3144, 2017 09 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Morphogen concentration gradients that extend across developmental fields form by dispersion from source cells. In the wing disc, Hedgehog (Hh) produced by posterior compartment cells distributes in a concentration gradient to adjacent cells of the anterior compartment. We monitored Hh:GFP after pulsed expression, and analyzed the movement and colocalization of Hh, Patched (Ptc) and Smoothened (Smo) proteins tagged with GFP or mCherry and expressed at physiological levels from bacterial artificial chromosome transgenes. Hh:GFP moved to basal subcellular locations prior to release from posterior compartment cells that express it, and was taken up by basal cytonemes that extend to the source cells. Hh and Ptc were present in puncta that moved along the basal cytonemes and formed characteristic apical-basal distributions in the anterior compartment cells. The basal cytonemes required , , and , and both the Hh gradient and Hh signaling declined under conditions in which the cytonemes were compromised. These findings show that in the wing disc, Hh distributions and signaling are dependent upon basal release and uptake, and on cytoneme-mediated movement. No evidence for apical dispersion was obtained.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Proteínas Hedgehog/metabolismo
Discos Imaginais/metabolismo
Asas de Animais/metabolismo
[Mh] Termos MeSH secundário: Animais
Padronização Corporal
Compartimento Celular
Cromossomos Artificiais Bacterianos/genética
Proteínas de Fluorescência Verde/metabolismo
Transporte Proteico
Transdução de Sinais
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Hedgehog Proteins); 147336-22-9 (Green Fluorescent Proteins); 149291-21-4 (hedgehog protein, Drosophila)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1242/dev.149856


  3 / 9712 MEDLINE  
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[PMID]:29190286
[Au] Autor:Tchelidze P; Benassarou A; Kaplan H; O'Donohue MF; Lucas L; Terryn C; Rusishvili L; Mosidze G; Lalun N; Ploton D
[Ad] Endereço:Faculty of Exact and Life Sciences, Department of Morphology, Tbilisi State University, Tbilisi, Georgia.
[Ti] Título:Nucleolar sub-compartments in motion during rRNA synthesis inhibition: Contraction of nucleolar condensed chromatin and gathering of fibrillar centers are concomitant.
[So] Source:PLoS One;12(11):e0187977, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nucleolus produces the large polycistronic transcript (47S precursor) containing the 18S, 5.8S and 28S rRNA sequences and hosts most of the nuclear steps of pre-rRNA processing. Among numerous components it contains condensed chromatin and active rRNA genes which adopt a more accessible conformation. For this reason, it is a paradigm of chromosome territory organization. Active rRNA genes are clustered within several fibrillar centers (FCs), in which they are maintained in an open configuration by Upstream Binding Factor (UBF) molecules. Here, we used the reproducible reorganization of nucleolar components induced by the inhibition of rRNA synthesis by Actinomycin D (AMD) to address the steps of the spatiotemporal reorganization of FCs and nucleolar condensed chromatin. To reach that goal, we used two complementary approaches: i) time-lapse confocal imaging of cells expressing one or several GFP-tagged proteins (fibrillarin, UBF, histone H2B) and ii) ultrastructural identification of nucleolar components involved in the reorganization. Data obtained by time lapse confocal microscopy were analyzed through detailed 3D imaging. This allowed us to demonstrate that AMD treatment induces no fusion and no change in the relative position of the different nucleoli contained in one nucleus. In contrast, for each nucleolus, we observed step by step gathering and fusion of both FCs and nucleolar condensed chromatin. To analyze the reorganization of FCs and condensed chromatin at a higher resolution, we performed correlative light and electron microscopy electron microscopy (CLEM) imaging of the same cells. We demonstrated that threads of intranucleolar condensed chromatin are localized in a complex 3D network of vacuoles. Upon AMD treatment, these structures coalesce before migrating toward the perinucleolar condensed chromatin, to which they finally fuse. During their migration, FCs, which are all linked to ICC, are pulled by the latter to gather as caps disposed at the periphery of nucleoli.
[Mh] Termos MeSH primário: Compartimento Celular
Nucléolo Celular/metabolismo
Cromatina/metabolismo
RNA Ribossômico/antagonistas & inibidores
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Dactinomicina/farmacologia
Seres Humanos
Microscopia Eletrônica de Transmissão
RNA Ribossômico/biossíntese
RNA Ribossômico/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (RNA, Ribosomal); 1CC1JFE158 (Dactinomycin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187977


  4 / 9712 MEDLINE  
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[PMID]:28873091
[Au] Autor:Flores SE; Aitchison A; Day AS; Keenan JI
[Ad] Endereço:Department of Surgery, University of Otago, Christchurch, New Zealand.
[Ti] Título:Helicobacter pylori infection perturbs iron homeostasis in gastric epithelial cells.
[So] Source:PLoS One;12(9):e0184026, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The iron deficiency anaemia that often accompanies infection with Helicobacter pylori may reflect increased uptake of iron into gastric epithelial cells. Here we show an infection-associated increase in total intracellular iron levels was associated with the redistribution of the transferrin receptor from the cell cytosol to the cell surface, and with increased levels of ferritin, an intracellular iron storage protein that corresponded with a significant increase in lysosomal stores of labile iron. In contrast, the pool of cytosolic labile iron was significantly decreased in infected cells. These changes in intracellular iron distribution were associated with the uptake and trafficking of H. pylori through the cells, and enhanced in strains capable of expressing the cagA virulence gene. We speculate that degradation of lysosomal ferritin may facilitate H. pylori pathogenesis, in addition to contributing to bacterial persistence in the human stomach.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Células Epiteliais/patologia
Infecções por Helicobacter/microbiologia
Infecções por Helicobacter/patologia
Helicobacter pylori/fisiologia
Homeostase
Ferro/metabolismo
Estômago/patologia
[Mh] Termos MeSH secundário: Antígenos de Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Compartimento Celular
Linhagem Celular Tumoral
Células Epiteliais/microbiologia
Ferritinas/metabolismo
Seres Humanos
Lisossomos/metabolismo
Mutação/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores da Transferrina/genética
Receptores da Transferrina/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (RNA, Messenger); 0 (Receptors, Transferrin); 0 (cagA protein, Helicobacter pylori); 152989-05-4 (rab7 protein); 9007-73-2 (Ferritins); E1UOL152H7 (Iron); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184026


  5 / 9712 MEDLINE  
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[PMID]:28807898
[Au] Autor:Carreno G; Apps JR; Lodge EJ; Panousopoulos L; Haston S; Gonzalez-Meljem JM; Hahn H; Andoniadou CL; Martinez-Barbera JP
[Ad] Endereço:Developmental Biology and Cancer Programme, Birth Defects Research Centre, Great Ormond Street Institute of Child Health, University College London, London WC1N 1EH, UK.
[Ti] Título:Hypothalamic sonic hedgehog is required for cell specification and proliferation of LHX3/LHX4 pituitary embryonic precursors.
[So] Source:Development;144(18):3289-3302, 2017 09 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sonic hedgehog (SHH) is an essential morphogenetic signal that dictates cell fate decisions in several developing organs in mammals. data suggest that SHH is required to specify LHX3 /LHX4 Rathke's pouch (RP) progenitor identity. However, studies have failed to reveal such a function, supporting instead a crucial role for SHH in promoting proliferation of these RP progenitors and for differentiation of pituitary cell types. Here, we have used a genetic approach to demonstrate that activation of the SHH pathway is necessary to induce LHX3 /LHX4 RP identity in mouse embryos. First, we show that conditional deletion of in the anterior hypothalamus results in a fully penetrant phenotype characterised by a complete arrest of RP development, with lack of expression in RP epithelium at 9.0 days post coitum (dpc) and total loss of pituitary tissue by 12.5 dpc. Conversely, overactivation of the SHH pathway by conditional deletion of in RP progenitors leads to severe hyperplasia and enlargement of the Sox2 stem cell compartment by the end of gestation.
[Mh] Termos MeSH primário: Linhagem da Célula
Proteínas Hedgehog/metabolismo
Hipotálamo/embriologia
Hipotálamo/metabolismo
Proteínas com Homeodomínio LIM/metabolismo
Hipófise/embriologia
Hipófise/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Compartimento Celular
Contagem de Células
Diferenciação Celular
Proliferação Celular
Células Clonais
Cruzamentos Genéticos
Ectoderma/embriologia
Ectoderma/metabolismo
Embrião de Mamíferos/metabolismo
Endoderma/embriologia
Endoderma/metabolismo
Epitélio/embriologia
Epitélio/metabolismo
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Proteínas Hedgehog/genética
Seres Humanos
Masculino
Mutação/genética
Hipófise/patologia
Transdução de Sinais
Células-Tronco
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hedgehog Proteins); 0 (LIM-Homeodomain Proteins); 0 (Lhx3 protein); 0 (Lhx4 protein, mouse); 0 (Shh protein, mouse); 0 (Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE
[do] DOI:10.1242/dev.153387


  6 / 9712 MEDLINE  
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[PMID]:28803967
[Au] Autor:Wang W; Perens EA; Oikonomou G; Wallace SW; Lu Y; Shaham S
[Ad] Endereço:Laboratory of Developmental Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
[Ti] Título:IGDB-2, an Ig/FNIII protein, binds the ion channel LGC-34 and controls sensory compartment morphogenesis in C. elegans.
[So] Source:Dev Biol;430(1):105-112, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sensory organ glia surround neuronal receptive endings (NREs), forming a specialized compartment important for neuronal activity, and reminiscent of glia-ensheathed synapses in the central nervous system. We previously showed that DAF-6, a Patched-related protein, is required in glia of the C. elegans amphid sensory organ to restrict sensory compartment size. LIT-1, a Nemo-like kinase, and SNX-1, a retromer component, antagonize DAF-6 and promote compartment expansion. To further explore the machinery underlying compartment size control, we sought genes whose inactivation restores normal compartment size to daf-6 mutants. We found that mutations in igdb-2, encoding a single-pass transmembrane protein containing Ig-like and fibronectin type III domains, suppress daf-6 mutant defects. IGDB-2 acts in glia, where it localizes to glial membranes surrounding NREs, and, together with LIT-1 and SNX-1, regulates compartment morphogenesis. Immunoprecipitation followed by mass spectrometry demonstrates that IGDB-2 binds to LGC-34, a predicted ligand-gated ion channel, and lgc-34 mutations inhibit igdb-2 suppression of daf-6. Our findings reveal a novel membrane protein complex and suggest possible mechanisms for how sensory compartment size is controlled.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Compartimento Celular
Morfogênese
Células Receptoras Sensoriais/citologia
Células Receptoras Sensoriais/metabolismo
[Mh] Termos MeSH secundário: Alelos
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/genética
Membrana Celular/metabolismo
Epistasia Genética
Genes Supressores
Células HEK293
Seres Humanos
Ligantes
Modelos Biológicos
Mutação/genética
Neuroglia/metabolismo
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Ligands)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE


  7 / 9712 MEDLINE  
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[PMID]:28683137
[Au] Autor:Shukla A; Bhattacharyya A; Kuppusamy L; Srivas M; Thattai M
[Ad] Endereço:School of Computer Science and Engineering, Vellore Institute of Technology, Vellore, India.
[Ti] Título:Discovering vesicle traffic network constraints by model checking.
[So] Source:PLoS One;12(7):e0180692, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A eukaryotic cell contains multiple membrane-bound compartments. Transport vesicles move cargo between these compartments, just as trucks move cargo between warehouses. These processes are regulated by specific molecular interactions, as summarized in the Rothman-Schekman-Sudhof model of vesicle traffic. The whole structure can be represented as a transport graph: each organelle is a node, and each vesicle route is a directed edge. What constraints must such a graph satisfy, if it is to represent a biologically realizable vesicle traffic network? Graph connectedness is an informative feature: 2-connectedness is necessary and sufficient for mass balance, but stronger conditions are required to ensure correct molecular specificity. Here we use Boolean satisfiability (SAT) and model checking as a framework to discover and verify graph constraints. The poor scalability of SAT model checkers often prevents their broad application. By exploiting the special structure of the problem, we scale our model checker to vesicle traffic systems with reasonably large numbers of molecules and compartments. This allows us to test a range of hypotheses about graph connectivity, which can later be proved in full generality by other methods.
[Mh] Termos MeSH primário: Compartimento Celular
Modelos Biológicos
Vesículas Transportadoras/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas SNARE/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SNARE Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180692


  8 / 9712 MEDLINE  
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[PMID]:28682332
[Au] Autor:Nagano T; Lubling Y; Várnai C; Dudley C; Leung W; Baran Y; Mendelson Cohen N; Wingett S; Fraser P; Tanay A
[Ad] Endereço:Nuclear Dynamics Programme, The Babraham Insitute, Cambridge CB22 3AT, UK.
[Ti] Título:Cell-cycle dynamics of chromosomal organization at single-cell resolution.
[So] Source:Nature;547(7661):61-67, 2017 07 05.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chromosomes in proliferating metazoan cells undergo marked structural metamorphoses every cell cycle, alternating between highly condensed mitotic structures that facilitate chromosome segregation, and decondensed interphase structures that accommodate transcription, gene silencing and DNA replication. Here we use single-cell Hi-C (high-resolution chromosome conformation capture) analysis to study chromosome conformations in thousands of individual cells, and discover a continuum of cis-interaction profiles that finely position individual cells along the cell cycle. We show that chromosomal compartments, topological-associated domains (TADs), contact insulation and long-range loops, all defined by bulk Hi-C maps, are governed by distinct cell-cycle dynamics. In particular, DNA replication correlates with a build-up of compartments and a reduction in TAD insulation, while loops are generally stable from G1 to S and G2 phase. Whole-genome three-dimensional structural models reveal a radial architecture of chromosomal compartments with distinct epigenomic signatures. Our single-cell data therefore allow re-interpretation of chromosome conformation maps through the prism of the cell cycle.
[Mh] Termos MeSH primário: Ciclo Celular/fisiologia
Cromossomos de Mamíferos/química
Cromossomos de Mamíferos/metabolismo
Epigênese Genética
Análise de Célula Única/métodos
[Mh] Termos MeSH secundário: Animais
Compartimento Celular
Ciclo Celular/genética
Cromossomos de Mamíferos/genética
Haploidia
Imagem Tridimensional
Camundongos
Células-Tronco Embrionárias Murinas/citologia
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1038/nature23001


  9 / 9712 MEDLINE  
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[PMID]:28648643
[Au] Autor:Kornmann B; Ungermann C
[Ad] Endereço:Swiss Institute of Technology Zurich (ETH Zurich), Switzerland. Electronic address: benoit.kornmann@bc.biol.ethz.ch.
[Ti] Título:Membrane contact sites.
[So] Source:Biochim Biophys Acta;1864(9):1435-1438, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Mh] Termos MeSH primário: Compartimento Celular
Membrana Celular/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Seres Humanos
Metabolismo dos Lipídeos
[Pt] Tipo de publicação:EDITORIAL; INTRODUCTORY JOURNAL ARTICLE
[Nm] Nome de substância:
SY7Q814VUP (Calcium)
[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:170627
[St] Status:MEDLINE


  10 / 9712 MEDLINE  
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[PMID]:28635326
[Au] Autor:Nichols RJ; Cassidy-Amstutz C; Chaijarasphong T; Savage DF
[Ad] Endereço:a Department of Molecular and Cell Biology , UC Berkeley , Berkeley , CA , USA.
[Ti] Título:Encapsulins: molecular biology of the shell.
[So] Source:Crit Rev Biochem Mol Biol;52(5):583-594, 2017 Oct.
[Is] ISSN:1549-7798
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Compartmentalization is both a fundamental principle of cellular organization and an emerging theme in prokaryotic biology. Work in the past few decades has shown that protein-based organelles called microcompartments enhance the function of encapsulated cargo proteins. More recently, the repertoire of known prokaryotic organelles has expanded beyond microcompartments to include a new class of smaller proteinaceous compartments, termed nanocompartments (also known as encapsulins). Nanocompartments are icosahedral capsids that are smaller and less complex than microcompartments. Encapsulins are formed by a single species of shell protein that self-assembles and typically encapsulates only one type of cargo protein. Significant progress has been made in understanding the structure of nanocompartment shells and the loading of cargo to the interior. Recent analysis has also demonstrated the prevalence of encapsulin genes throughout prokaryotic genomes and documented a large diversity of cargo proteins with a variety of novel functions, suggesting that nanocompartments play an important role in many microbes. Here we review the current understanding of encapsulin structure and function and highlight exciting open questions of physiological significance.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Compartimento Celular
Organelas
[Mh] Termos MeSH secundário: Fenômenos Fisiológicos Bacterianos
Proteínas de Bactérias/fisiologia
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1080/10409238.2017.1337709



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