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[PMID]:29292422
[Au] Autor:Zakeri B; Niebling S; Martinéz AG; Sokkar P; Sanchez-Garcia E; Schmuck C; Schlücker S
[Ad] Endereço:Physical Chemistry, University of Duisburg-Essen, 45141 Essen, Germany. sebastian.schluecker@uni-due.de.
[Ti] Título:Molecular recognition of carboxylates in the protein leucine zipper by a multivalent supramolecular ligand: residue-specific, sensitive and label-free probing by UV resonance Raman spectroscopy.
[So] Source:Phys Chem Chem Phys;20(3):1817-1820, 2018 Jan 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ultraviolet resonance Raman (UVRR) spectroscopy is a selective, sensitive and label-free vibrational spectroscopic technique. Here, we demonstrate as proof of concept that UVRR can be used for probing the recognition between a multivalent supramolecular ligand and acidic residues in leucine zipper, an α-helical structural motif of many proteins.
[Mh] Termos MeSH primário: Ligantes
Proteínas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Dimerização
Zíper de Leucina
Simulação de Dinâmica Molecular
Estrutura Secundária de Proteína
Proteínas/metabolismo
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Proteins)
[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:180103
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp04971d


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[PMID]:28615210
[Au] Autor:Loftus MS; Verville N; Kedes DH
[Ad] Endereço:Department of Microbiology, Immunology, and Cancer Biology, University of Virginia, Charlottesville, Virginia, USA.
[Ti] Título:A Conserved Leucine Zipper Motif in Gammaherpesvirus ORF52 Is Critical for Distinct Microtubule Rearrangements.
[So] Source:J Virol;91(17), 2017 Sep 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Productive viral infection often depends on the manipulation of the cytoskeleton. Herpesviruses, including rhesus monkey rhadinovirus (RRV) and its close homolog, the oncogenic human gammaherpesvirus Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 (KSHV/HHV8), exploit microtubule (MT)-based retrograde transport to deliver their genomes to the nucleus. Subsequently, during the lytic phase of the life cycle, the maturing viral particles undergo orchestrated translocation to specialized regions within the cytoplasm, leading to tegumentation, secondary envelopment, and then egress. As a result, we hypothesized that RRV might induce changes in the cytoskeleton at both early and late stages of infection. Using confocal imaging, we found that RRV infection led to the thickening and acetylation of MTs emanating from the MT-organizing center (MTOC) shortly after viral entry and more pronounced and diffuse MT reorganization during peak stages of lytic gene expression and virion production. We subsequently identified open reading frame 52 (ORF52), a multifunctional and abundant tegument protein, as being the only virally encoded component responsible for these cytoskeletal changes. Mutational and modeling analyses indicated that an evolutionarily conserved, truncated leucine zipper motif near the N terminus as well as a strictly conserved arginine residue toward the C terminus of ORF52 play critical roles in its ability to rearrange the architecture of the MT cytoskeleton. Taken together, our findings combined with data from previous studies describing diverse roles for ORF52 suggest that it likely binds to different cellular components, thereby allowing context-dependent modulation of function. A thorough understanding of the processes governing viral infection includes knowledge of how viruses manipulate their intracellular milieu, including the cytoskeleton. Altering the dynamics of actin or MT polymerization, for example, is a common strategy employed by viruses to ensure efficient entry, maturation, and egress as well as the avoidance of antiviral defenses through the sequestration of key cellular factors. We found that infection with RRV, a homolog of the human pathogen KSHV, led to perinuclear wrapping by acetylated MT bundles and identified ORF52 as the viral protein underlying these changes. Remarkably, incoming virions were able to supply sufficient ORF52 to induce MT thickening and acetylation near the MTOC, potentially aiding in the delivery viral genomes to the nucleus. Although the function of MT alterations during late stages of infection requires further study, ORF52 shares functional and structural similarities with alphaherpesvirus VP22, underscoring the evolutionary importance of MT cytoskeletal manipulations for this virus family.
[Mh] Termos MeSH primário: Zíper de Leucina
Centro Organizador dos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Rhadinovirus/genética
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Núcleo Celular/virologia
Fibroblastos/virologia
Zíper de Leucina/genética
Macaca mulatta
Centro Organizador dos Microtúbulos/virologia
Microtúbulos/virologia
Fases de Leitura Aberta
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE


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[PMID]:28422996
[Au] Autor:Guan X; Li Z; Zhang Z; Wei X; Xie J; Chen J; Chen Q
[Ad] Endereço:College of Horticulture, Fujian Agriculture and Forestry University, Fuzhou, Fujian, China.
[Ti] Título:Overexpression of an EaZIP gene devoid of transit peptide sequence induced leaf variegation in tobacco.
[So] Source:PLoS One;12(4):e0175995, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leaf variegation is an ornamental trait that is not only biologically but also economically important. In our previous study, a Mg-protoporphyrin IX monomethyl ester cyclase homologue, EaZIP (Epipremnum aureum leucine zipper) was found to be associated with leaf variegation in Epipremnum aureum (Linden & Andre) G.S. Bunting. The protein product of this nuclear-encoded gene is targeted back to chloroplast involving in chlorophyll biosynthesis. Based on a web-based homology analysis, the EaZIP was found to lack a chloroplast transit peptide (cTP) sequence. In the present study, we tested if overexpression of the EaZIP cDNA with or without the cTP sequence could affect leaf variegation. Transgenic tobacco plants overexpressing EaZIP genes with (EaZIPwcTP) and without (EaZIPwocTP) cTP sequence were generated. Many plant lines harboring EaZIPwocTP showed variegated leaves, while none of the plant lines with EaZIPwcTP produced such a phenotype. Molecular analysis of T0 plants and selfed T1 progeny, as well as observations of tagged marker GFP (green fluorescent protein) did not show any other difference in patterns of gene integrity and expression. Results from this study indicate that transgenic approach for expressing EaZIPwocTP could be a novel method of generating variegated plants even through the underlying mechanisms remain to be elucidated.
[Mh] Termos MeSH primário: Proteínas de Cloroplastos/genética
Regulação da Expressão Gênica de Plantas
Folhas de Planta/genética
Proteínas de Plantas/genética
Sinais Direcionadores de Proteínas/genética
Tabaco/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Araceae/genética
Araceae/metabolismo
Sequência de Bases
Núcleo Celular/genética
Núcleo Celular/metabolismo
Proteínas de Cloroplastos/metabolismo
Cloroplastos/genética
Cloroplastos/metabolismo
DNA Complementar/genética
DNA Complementar/metabolismo
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Zíper de Leucina
Fenótipo
Folhas de Planta/anatomia & histologia
Folhas de Planta/metabolismo
Proteínas de Plantas/metabolismo
Plantas Geneticamente Modificadas
Alinhamento de Sequência
Tabaco/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chloroplast Proteins); 0 (DNA, Complementary); 0 (Plant Proteins); 0 (Protein Sorting Signals); 0 (Transcription Factors); 0 (chloroplast transit peptides)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175995


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[PMID]:28337836
[Au] Autor:Perotti MF; Ribone PA; Chan RL
[Ad] Endereço:Instituto de Agrobiotecnología del Litoral Universidad Nacional del Litoral, CONICET, Centro Científico Tecnológico CONICET Santa Fe, Santa Fe, Argentina.
[Ti] Título:Plant transcription factors from the homeodomain-leucine zipper family I. Role in development and stress responses.
[So] Source:IUBMB Life;69(5):280-289, 2017 May.
[Is] ISSN:1521-6551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In front of stressful conditions plants display adaptation mechanisms leading to changes in their morphology, physiology, development and molecular composition. Transcription factors (TFs) play crucial roles in these complex adaptation processes. This work is focused in the homeodomain-leucine zipper I (HD-Zip I) family of TFs, unique to plants. First discovered in 1991, they were identified and isolated from monocotyledonous and dicotyledonous plants showing high structural similarity and diversified functions. These TFs have, besides the homeodomain and leucine zipper, conserved motifs in their carboxy-termini allowing the interaction with the basal machinery and with other regulatory proteins. The model dicotyledonous plant Arabidopsis thaliana has 17 HD-Zip I members; most of them regulated by external stimuli and hormones. These TFs are involved in key developmental processes like root and stem elongation, rosette leaves morphology determination, inflorescence stem branching, flowering and pollen hydration. Moreover, they are key players in responses to environmental stresses and illumination conditions. Several HD-Zip I encoding genes from different species were protected in patents because their overexpression or mutation generates improved agronomical phenotypes. Here we discuss many aspects about these TFs including structural features, biological functions and their utilization as biotechnological tools to improve crops. © 2017 IUBMB Life, 69(5):280-289, 2017.
[Mh] Termos MeSH primário: Desenvolvimento Vegetal
Proteínas de Plantas/metabolismo
Estresse Fisiológico
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/metabolismo
Biotecnologia/métodos
Regulação da Expressão Gênica de Plantas
Proteínas de Homeodomínio/metabolismo
Zíper de Leucina
Família Multigênica
Mutação
Proteínas de Plantas/química
Proteínas de Plantas/genética
Plantas/genética
Fatores de Transcrição/química
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (Plant Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1002/iub.1619


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[PMID]:28280239
[Au] Autor:Sharma AK; Birrane G; Anklin C; Rigby AC; Alper SL
[Ad] Endereço:From the Division of Nephrology and Center for Vascular Biology Research, aksharma@bidmc.harvard.edu namasal34@gmail.com.
[Ti] Título:NMR insight into myosin-binding subunit coiled-coil structure reveals binding interface with protein kinase G-Iα leucine zipper in vascular function.
[So] Source:J Biol Chem;292(17):7052-7065, 2017 Apr 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitrovasodilators relax vascular smooth-muscle cells in part by modulating the interaction of the C-terminal coiled-coil domain (CC) and/or the leucine zipper (LZ) domain of the myosin light-chain phosphatase component, myosin-binding subunit (MBS), with the N-terminal LZ domain of protein kinase G (PKG)-Iα. Despite the importance of vasodilation in cardiovascular homeostasis and therapy, our structural understanding of the MBS CC interaction with LZ PKG-1α has remained limited. Here, we report the 3D NMR solution structure of homodimeric CC MBS in which amino acids 932-967 form a coiled-coil of two monomeric α-helices in parallel orientation. We found that the structure is stabilized by non-covalent interactions, with dominant contributions from hydrophobic residues at and heptad positions. Using NMR chemical-shift perturbation (CSP) analysis, we identified a subset of hydrophobic and charged residues of CC MBS (localized within and adjacent to the C-terminal region) contributing to the dimer-dimer interaction interface between homodimeric CC MBS and homodimeric LZ PKG-Iα. N backbone relaxation NMR revealed the dynamic features of the CC MBS interface residues identified by NMR CSP. Paramagnetic relaxation enhancement- and CSP-NMR-guided HADDOCK modeling of the dimer-dimer interface of the heterotetrameric complex exhibits the involvement of non-covalent intermolecular interactions that are localized within and adjacent to the C-terminal regions of each homodimer. These results deepen our understanding of the binding restraints of this CC MBS·LZ PKG-Iα low-affinity heterotetrameric complex and allow reevaluation of the role(s) of myosin light-chain phosphatase partner polypeptides in regulation of vascular smooth-muscle cell contractility.
[Mh] Termos MeSH primário: Proteína Quinase Dependente de GMP Cíclico Tipo I/química
Zíper de Leucina
Miosinas/química
[Mh] Termos MeSH secundário: Animais
Dicroísmo Circular
Interações Hidrofóbicas e Hidrofílicas
Espectroscopia de Ressonância Magnética
Camundongos
Simulação de Dinâmica Molecular
Músculo Liso Vascular/citologia
Ligação Proteica
Domínios Proteicos
Multimerização Proteica
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Espectrofotometria Ultravioleta
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.11.12 (Cyclic GMP-Dependent Protein Kinase Type I); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781260


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[PMID]:28251315
[Au] Autor:Chen E; Zhang X; Yang Z; Wang X; Yang Z; Zhang C; Wu Z; Kong D; Liu Z; Zhao G; Butt HI; Zhang X; Li F
[Ad] Endereço:State Key Laboratory of Cotton Biology, Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang, 455000, China.
[Ti] Título:Genome-wide analysis of the HD-ZIP IV transcription factor family in Gossypium arboreum and GaHDG11 involved in osmotic tolerance in transgenic Arabidopsis.
[So] Source:Mol Genet Genomics;292(3):593-609, 2017 Jun.
[Is] ISSN:1617-4623
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:HD-ZIP IV proteins belong to the homeodomain-leucine zipper (HD-ZIP) transcription factor family and are involved in trichome development and drought stress in plants. Although some functions of the HD-ZIP IV group are well understood in Arabidopsis, little is known about their function in cotton. In this study, HD-ZIP genes were identified from three Gossypium species (G. arboreum, G. raimondii and G. hirsutum) and clustered into four families (HD-ZIP I, II, III and IV) to separate HD-ZIP IV from the other three families. Systematic analyses of phylogeny, gene structure, conserved domains, and expression profiles in different plant tissues and the expression patterns under osmotic stress in leaves were further conducted in G. arboreum. More importantly, ectopic overexpression of GaHDG11, a representative of the HD-ZIP IV family, confers enhanced osmotic tolerance in transgenic Arabidopsis plants, possibly due to elongated primary root length, lower water loss rates, high osmoprotectant proline levels, significant levels of antioxidants CAT, and/or SOD enzyme activity with reduced levels of MDA. Taken together, these observations may lay the foundation for future functional analysis of cotton HD-ZIP IV genes to unravel their biological roles in cotton.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Gossypium/genética
Proteínas de Homeodomínio/genética
Zíper de Leucina/genética
Pressão Osmótica/fisiologia
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Catalase/metabolismo
Mapeamento Cromossômico
Secas
Regulação da Expressão Gênica de Plantas
Estudo de Associação Genômica Ampla
Plantas Geneticamente Modificadas/genética
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (HD-Zip protein, Arabidopsis); 0 (HDG11 protein, Arabidopsis); 0 (Homeodomain Proteins); 0 (Transcription Factors); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1007/s00438-017-1293-5


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[PMID]:28250114
[Au] Autor:Yu FH; Huang KJ; Wang CT
[Ad] Endereço:Department of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan.
[Ti] Título:C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain.
[So] Source:J Virol;91(10), 2017 May 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HIV-1 protease (PR) functions as a homodimer mediating virus maturation following virus budding. Gag-Pol dimerization is believed to trigger embedded PR activation by promoting PR dimer formation. Early PR activation can lead to markedly reduced virus yields due to premature Gag cleavage. The p6* peptide, located between Gag and PR, is believed to ensure virus production by preventing early PR maturation. Studies aimed at finding supporting evidence for this proposal are limited due to a reading frame overlap between p6* and the p6gag budding domain. To determine if p6* affects virus production via the modulation of PR activation, we engineered multiple constructs derived from Dp6*PR (an assembly- and processing-competent construct with Pol fused at the inactivated PR C terminus). The data indicated that a p6* deletion adjacent to active PR significantly impaired virus processing. We also observed that the insertion of a leucine zipper (LZ) dimerization motif in the deleted region eliminated virus production in a PR activity-dependent manner, suggesting that the LZ insertion triggered premature PR activation by facilitating PR dimer formation. As few as four C-terminal p6* residues remaining at the p6*/PR junction were sufficient to restore virus yields, with a Gag processing profile similar to that of the wild type. Our study provides supporting evidence in a virus assembly context that the C-terminal p6* tetrapeptide plays a role in preventing premature PR maturation. Supporting evidence for the assumption that p6* retards PR maturation in the context of virus assembly is lacking. We found that replacing p6* with a leucine zipper peptide abolished virus assembly due to the significant enhancement of Gag cleavage. However, as few as four C-terminal p6* residues remaining in the deleted region were sufficient for significant PR release, as well as for counteracting leucine zipper-incurred premature Gag cleavage. Our data provide evidence that (i) p6* ensures virus assembly by preventing early PR activation and (ii) four C-terminal p6* residues are critical for modulating PR activation. Current PR inhibitor development efforts are aimed largely at mature PR, but there is a tendency for HIV-1 variants that are resistant to multiple protease inhibitors to emerge. Our data support the idea of modulating PR activation by targeting PR precursors as an alternative approach to controlling HIV-1/AIDS.
[Mh] Termos MeSH primário: Protease de HIV/metabolismo
Zíper de Leucina
Produtos do Gene gag do Vírus da Imunodeficiência Humana/genética
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Fusão gag-pol/genética
Proteínas de Fusão gag-pol/metabolismo
Protease de HIV/genética
HIV-1/enzimologia
HIV-1/fisiologia
Zíper de Leucina/genética
Deleção de Sequência
Montagem de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Proteins, gag-pol); 0 (gag Gene Products, Human Immunodeficiency Virus); EC 3.4.23.- (HIV Protease); EC 3.4.23.- (p16 protease, Human immunodeficiency virus 1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE


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[PMID]:28249019
[Au] Autor:Ding Z; Fu L; Yan Y; Tie W; Xia Z; Wang W; Peng M; Hu W; Zhang J
[Ad] Endereço:Key Laboratory of Biology and Genetic Resources of Tropical Crops, Institute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural Sciences, Haikou, Hainan, China.
[Ti] Título:Genome-wide characterization and expression profiling of HD-Zip gene family related to abiotic stress in cassava.
[So] Source:PLoS One;12(3):e0173043, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Homeodomain-leucine zipper (HD-Zip) gene family plays important roles in various abiotic stresses and hormone signaling in plants. However, no information is currently available regarding this family in cassava (Manihot esculenta), an important drought-tolerant crop in tropical and sub-tropical areas. Here, 57 HD-Zip genes (MeHDZ01-57) were identified in the cassava genome, and they were classified into four subfamilies based on phylogenetic analysis, which was further supported by their gene structure and conserved motif characteristics. Of which five gene pairs were involved in segmental duplication but none for tandem duplication, suggesting that segmental duplication was the main cause for the expansion of MeHDZ gene family in cassava. Global expression profiles revealed that MeHDZ genes were constitutively expressed, or not expressed, or tissue-specific expressed in examined tissues in both cultivated and wild subspecies. Transcriptomic analysis of three genotypes showed that most of MeHDZ genes responded differently to drought and polyethylene glycol treatments. Subsequently, quantitative RT-PCR analysis revealed comprehensive responses of twelve selected MeHDZ genes to various stimuli including cold, salt, and ABA treatments. These findings will increase our understanding of HD-Zip gene family involved in abiotic stresses and signaling transduction, and will provide a solid base for further functional characterization of MeHDZ genes in cassava.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas
Proteínas de Homeodomínio/genética
Manihot/genética
Proteínas de Plantas/genética
Estresse Fisiológico
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Temperatura Baixa
Secas
Genoma de Planta
Genótipo
Proteínas de Homeodomínio/metabolismo
Zíper de Leucina
Manihot/metabolismo
Família Multigênica
Proteínas de Plantas/metabolismo
Salinidade
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (Plant Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173043


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[PMID]:28241402
[Au] Autor:Jakobson CM; Slininger Lee MF; Tullman-Ercek D
[Ad] Endereço:Department of Chemical and Biological Engineering, Northwestern University, Evanston, Illinois, 60208.
[Ti] Título:De novo design of signal sequences to localize cargo to the 1,2-propanediol utilization microcompartment.
[So] Source:Protein Sci;26(5):1086-1092, 2017 May.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Organizing heterologous biosyntheses inside bacterial cells can alleviate common problems owing to toxicity, poor kinetic performance, and cofactor imbalances. A subcellular organelle known as a bacterial microcompartment, such as the 1,2-propanediol utilization microcompartment of Salmonella, is a promising chassis for this strategy. Here we demonstrate de novo design of the N-terminal signal sequences used to direct cargo to these microcompartment organelles. We expand the native repertoire of signal sequences using rational and library-based approaches and show that a canonical leucine-zipper motif can function as a signal sequence for microcompartment localization. Our strategy can be applied to generate new signal sequences localizing arbitrary cargo proteins to the 1,2-propanediol utilization microcompartments.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Propilenoglicol/metabolismo
Engenharia de Proteínas
Sinais Direcionadores de Proteínas/genética
Salmonella typhimurium
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Zíper de Leucina/genética
Transporte Proteico/genética
Salmonella typhimurium/genética
Salmonella typhimurium/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Protein Sorting Signals); 6DC9Q167V3 (Propylene Glycol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3144


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[PMID]:28204810
[Au] Autor:Ma Y; Zhang B; Wang D; Qian L; Song X; Wang X; Yang C; Zhao G
[Ad] Endereço:Henan Medical College, Zhengzhou, Henan 451191, P.R. China.
[Ti] Título:HTLV-1 basic leucine zipper factor downregulates cyclin D1 expression via interactions with NF-κB.
[So] Source:Int J Mol Med;39(3):764-770, 2017 Mar.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Human T cell leukemia virus type 1 (HTLV-1) is an oncogenic retrovirus. It can cause adult T cell leukemia (ATL) and other diseases. The HTLV-1 basic leucine zipper (bZIP) factor (HBZ), which is encoded by the minus-strand of the provirus, is expressed in all cases of ATL and involved in T cell proliferation. However, the exact mechanism underlying its growth-promoting activity is poorly understood. Herein, we demonstrated that HBZ suppressed cyclin D1 expression by inhibiting the nuclear factor (NF)-κB signaling pathway. Among the potential mechanisms of cyclin D1 inhibition mediated by HBZ, we found that HBZ suppressed cyclin D1 promoter activity. Luciferase assay analysis revealed that HBZ repressed cyclin D1 promoter activity by suppressing NF-κB­driven transcription mediated by the p65 subunit. Using an immunoprecipitation assay, we found that HBZ could bind to p65, but not p50. Finally, we showed that HBZ selectively interacted with p65 via its AD+bZIP domains. By suppressing cyclin D1 expression, HBZ can alter cell cycle progression of HTLV-1-infected cells, which may be critical for oncogenesis.
[Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina Básica/metabolismo
Ciclina D1/genética
Regulação da Expressão Gênica
Vírus 1 Linfotrópico T Humano/fisiologia
NF-kappa B/metabolismo
Proteínas dos Retroviridae/metabolismo
[Mh] Termos MeSH secundário: Fatores de Transcrição de Zíper de Leucina Básica/química
Linhagem Celular
Ordem dos Genes
Vetores Genéticos/genética
Seres Humanos
Zíper de Leucina
Regiões Promotoras Genéticas
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas dos Retroviridae/química
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic-Leucine Zipper Transcription Factors); 0 (HBZ protein, human T-cell leukemia virus type I); 0 (NF-kappa B); 0 (Retroviridae Proteins); 136601-57-5 (Cyclin D1)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2017.2868



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