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  1 / 1095 MEDLINE  
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[PMID]:28470425
[Au] Autor:Ranawat P; Rawat S
[Ad] Endereço:Department of Botany and Microbiology, Hemvati Nandan Bahuguna Garhwal University, Srinagar (Garhwal), Uttrakhand, India.
[Ti] Título:Radiation resistance in thermophiles: mechanisms and applications.
[So] Source:World J Microbiol Biotechnol;33(6):112, 2017 Jun.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The study of prokaryotic life in high temperature environments viz., geothermal areas, hot, acidic geysers and undersea hydrothermal vents has revealed the existence of thermophiles (or hyperthermophiles). These microorganisms possess various stress adaptation mechanisms which enable them to bypass multiple physical and chemical barriers for survival. The discovery of radiation resistant thermophile Deinococcus geothermalis has given new insights into the field of radiation microbiology. The ability of radiation resistant thermophiles to deal with the lethal effects of ionizing radiations like DNA damage, oxidative bursts and protein damage has made them a model system for exobiology and interplanetary transmission of life. They might be an antiquity of historical transport process that brought microbial life on Earth. These radiation resistant thermophiles are resistant to desiccation as well and maintain their homeostasis by advance DNA repair mechanisms, reactive oxygen species (ROS) detoxification system and accumulation of compatible solutes. Moreover, engineered radioresistant thermophilic strains are the best candidate for bioremediation of radionuclide waste while the extremolytes produced by these organisms may have predicted therapeutic uses. So, the present article delineate a picture of radiation resistance thermophiles, their adaptive mechanisms to evade stress viz., radiation and desiccation, their present applications along with new horizons in near future.
[Mh] Termos MeSH primário: Archaea/fisiologia
Archaea/efeitos da radiação
Bactérias/efeitos da radiação
Fenômenos Fisiológicos Bacterianos/efeitos da radiação
Temperatura Alta
[Mh] Termos MeSH secundário: Actinobacteria/fisiologia
Actinobacteria/efeitos da radiação
Bactérias/genética
Fenômenos Fisiológicos Bacterianos/genética
Biodegradação Ambiental
Cianobactérias/fisiologia
Cianobactérias/efeitos da radiação
Dano ao DNA/efeitos da radiação
Reparo do DNA
Deinococcus/genética
Deinococcus/fisiologia
Deinococcus/efeitos da radiação
Microbiologia Ambiental
Exobiologia
Halobacterium/fisiologia
Halobacterium/efeitos da radiação
Pyrococcus/fisiologia
Pyrococcus/efeitos da radiação
Radiação Ionizante
Espécies Reativas de Oxigênio/efeitos da radiação
Explosão Respiratória/efeitos da radiação
Estresse Fisiológico
Sulfolobus/fisiologia
Sulfolobus/efeitos da radiação
Thermococcus/fisiologia
Thermococcus/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Reactive Oxygen Species)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171201
[Lr] Data última revisão:
171201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2279-5


  2 / 1095 MEDLINE  
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[PMID]:28977519
[Au] Autor:Han W; Pan S; López-Méndez B; Montoya G; She Q
[Ad] Endereço:Archaea Center, Department of Biology, University of Copenhagen, Ole Maal?es Vej 5, Copenhagen Biocenter, DK-2200 Copenhagen N, Denmark.
[Ti] Título:Allosteric regulation of Csx1, a type IIIB-associated CARF domain ribonuclease by RNAs carrying a tetraadenylate tail.
[So] Source:Nucleic Acids Res;45(18):10740-10750, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CRISPR-Cas systems protect prokaryotes against invading viruses and plasmids. The system is associated with a large number of Cas accessory proteins among which many contain a CARF (CRISPR-associated Rossmann fold) domain implicated in ligand binding and a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) nuclease domain. Here, such a dual domain protein, i.e. the Sulfolobus islandicus Csx1 (SisCsx1) was characterized. The enzyme exhibited metal-independent single-strand specific ribonuclease activity. In fact, SisCsx1 showed a basal RNase activity in the absence of ligand; upon the binding of an RNA ligand carrying four continuous adenosines at the 3'-end (3'-tetra-rA), the activated SisCsx1 degraded RNA substrate with a much higher turnover rate. Amino acid substitution mutants of SisCsx1 were obtained, and characterization of these mutant proteins showed that the CARF domain of the enzyme is responsible for binding to 3'-tetra-rA and the ligand binding strongly activates RNA cleavage by the HEPN domain. Since RNA polyadenylation is an important step in RNA decay in prokaryotes, and poly(A) RNAs can activate CARF domain proteins, the poly(A) RNA may function as an important signal in the cellular responses to viral infection and environmental stimuli, leading to degradation of both viral and host transcripts and eventually to cell dormancy or cell death.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Endorribonucleases/metabolismo
RNA Mensageiro/química
Sulfolobus/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Proteínas Arqueais/química
Endorribonucleases/química
Ligantes
Metais/metabolismo
Poli A/química
Ligação Proteica
Domínios Proteicos
Clivagem do RNA
Sulfolobus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Ligands); 0 (Metals); 0 (RNA, Messenger); 24937-83-5 (Poly A); EC 3.1.- (Endoribonucleases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx726


  3 / 1095 MEDLINE  
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[PMID]:28973046
[Au] Autor:Visone V; Han W; Perugino G; Del Monaco G; She Q; Rossi M; Valenti A; Ciaramella M
[Ad] Endereço:Institute of Biosciences and Bioresources, National Research Council of Italy, Napoli, Italy.
[Ti] Título:In vivo and in vitro protein imaging in thermophilic archaea by exploiting a novel protein tag.
[So] Source:PLoS One;12(10):e0185791, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein imaging, allowing a wide variety of biological studies both in vitro and in vivo, is of great importance in modern biology. Protein and peptide tags fused to proteins of interest provide the opportunity to elucidate protein location and functions, detect protein-protein interactions, and measure protein activity and kinetics in living cells. Whereas several tags are suitable for protein imaging in mesophilic organisms, the application of this approach to microorganisms living at high temperature has lagged behind. Archaea provide an excellent and unique model for understanding basic cell biology mechanisms. Here, we present the development of a toolkit for protein imaging in the hyperthermophilic archaeon Sulfolobus islandicus. The system relies on a thermostable protein tag (H5) constructed by engineering the alkylguanine-DNA-alkyl-transferase protein of Sulfolobus solfataricus, which can be covalently labeled using a wide range of small molecules. As a suitable host, we constructed, by CRISPR-based genome-editing technology, a S. islandicus mutant strain deleted for the alkylguanine-DNA-alkyl-transferase gene (Δogt). Introduction of a plasmid-borne H5 gene in this strain led to production of a functional H5 protein, which was successfully labeled with appropriate fluorescent molecules and visualized in cell extracts as well as in Δogt live cells. H5 was fused to reverse gyrase, a peculiar thermophile-specific DNA topoisomerase endowed with positive supercoiling activity, and allowed visualization of the enzyme in living cells. To the best of our knowledge, this is the first report of in vivo imaging of any protein of a thermophilic archaeon, filling an important gap in available tools for cell biology studies in these organisms.
[Mh] Termos MeSH primário: Archaea/metabolismo
Proteínas Arqueais/metabolismo
Sulfolobus solfataricus/metabolismo
Sulfolobus/metabolismo
[Mh] Termos MeSH secundário: DNA Topoisomerases Tipo I/metabolismo
Temperatura Alta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); EC 5.99.1.2 (DNA Topoisomerases, Type I)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185791


  4 / 1095 MEDLINE  
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[PMID]:28934494
[Au] Autor:Oscorbin IP; Belousova EA; Boyarskikh UA; Zakabunin AI; Khrapov EA; Filipenko ML
[Ad] Endereço:Laboratory of Pharmacogenomics, Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Lavrentiev Avenue 8, Novosibirsk 630090, Russian Federation.
[Ti] Título:Derivatives of Bst-like Gss-polymerase with improved processivity and inhibitor tolerance.
[So] Source:Nucleic Acids Res;45(16):9595-9610, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:At the moment, one of the actual trends in medical diagnostics is a development of methods for practical applications such as point-of-care testing, POCT or research tools, for example, whole genome amplification, WGA. All the techniques are based on using of specific DNA polymerases having strand displacement activity, high synthetic processivity, fidelity and, most significantly, tolerance to contaminants, appearing from analysed biological samples or collected under purification procedures. Here, we have designed a set of fusion enzymes based on catalytic domain of DNA polymerase I from Geobacillus sp. 777 with DNA-binding domain of DNA ligase Pyrococcus abyssi and Sto7d protein from Sulfolobus tokodaii, analogue of Sso7d. Designed chimeric DNA polymerases DBD-Gss, Sto-Gss and Gss-Sto exhibited the same level of thermal stability, thermal transferase activity and fidelity as native Gss; however, the processivity was increased up to 3-fold, leading to about 4-fold of DNA product in WGA which is much more exiting. The attachment of DNA-binding proteins enhanced the inhibitor tolerance of chimeric polymerases in loop-mediated isothermal amplification to several of the most common DNA sample contaminants-urea and whole blood, heparin, ethylenediaminetetraacetic acid, NaCl, ethanol. Therefore, chimeric Bst-like Gss-polymerase will be promising tool for both WGA and POCT due to increased processivity and inhibitor tolerance.
[Mh] Termos MeSH primário: DNA Polimerase I/metabolismo
Geobacillus/enzimologia
Engenharia de Proteínas/métodos
Proteínas Recombinantes de Fusão/genética
[Mh] Termos MeSH secundário: Domínio Catalítico
Clonagem Molecular
DNA/metabolismo
DNA Polimerase I/antagonistas & inibidores
DNA Polimerase I/genética
Inibidores Enzimáticos/farmacologia
Genoma Humano
Geobacillus/genética
Geobacillus stearothermophilus/enzimologia
Geobacillus stearothermophilus/genética
Seres Humanos
Técnicas de Amplificação de Ácido Nucleico/métodos
Estabilidade Proteica
Pyrococcus abyssi/genética
Proteínas Recombinantes de Fusão/metabolismo
Sulfolobus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Recombinant Fusion Proteins); 9007-49-2 (DNA); EC 2.7.7.- (DNA Polymerase I)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx645


  5 / 1095 MEDLINE  
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[PMID]:28911114
[Au] Autor:Liu T; Liu Z; Ye Q; Pan S; Wang X; Li Y; Peng W; Liang Y; She Q; Peng N
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, P.R. China.
[Ti] Título:Coupling transcriptional activation of CRISPR-Cas system and DNA repair genes by Csa3a in Sulfolobus islandicus.
[So] Source:Nucleic Acids Res;45(15):8978-8992, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CRISPR-Cas system provides the adaptive immunity against invading genetic elements in prokaryotes. Recently, we demonstrated that Csa3a regulator mediates spacer acquisition in Sulfolobus islandicus by activating the expression of Type I-A adaptation cas genes. However, links between the activation of spacer adaptation and CRISPR transcription/processing, and the requirement for DNA repair genes during spacer acquisition remained poorly understood. Here, we demonstrated that de novo spacer acquisition required Csa1, Cas1, Cas2 and Cas4 proteins of the Sulfolobus Type I-A system. Disruption of genes implicated in crRNA maturation or DNA interference led to a significant accumulation of acquired spacers, mainly derived from host genomic DNA. Transcriptome and proteome analyses showed that Csa3a activated expression of adaptation cas genes, CRISPR RNAs, and DNA repair genes, including herA helicase, nurA nuclease and DNA polymerase II genes. Importantly, Csa3a specifically bound the promoters of the above DNA repair genes, suggesting that they were directly activated by Csa3a for adaptation. The Csa3a regulator also specifically bound to the leader sequence to activate CRISPR transcription in vivo. Our data indicated that the Csa3a regulator couples transcriptional activation of the CRISPR-Cas system and DNA repair genes for spacer adaptation and efficient interference of invading genetic elements.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Sistemas CRISPR-Cas
Reparo do DNA
DNA Arqueal/genética
Regulação da Expressão Gênica em Archaea
Sulfolobus/genética
Ativação Transcricional
[Mh] Termos MeSH secundário: Proteínas Arqueais/imunologia
Sequência de Bases
Proteínas Associadas a CRISPR/genética
Proteínas Associadas a CRISPR/imunologia
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
DNA Helicases/genética
DNA Helicases/imunologia
DNA Polimerase II/genética
DNA Polimerase II/imunologia
DNA Arqueal/imunologia
Endodesoxirribonucleases/genética
Endodesoxirribonucleases/imunologia
Chaperonas Moleculares/genética
Chaperonas Moleculares/imunologia
Regiões Promotoras Genéticas
Alinhamento de Sequência
Homologia de Sequência do Ácido Nucleico
Sulfolobus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (CRISPR-Associated Proteins); 0 (DNA, Archaeal); 0 (Molecular Chaperones); EC 2.7.7.- (DNA Polymerase II); EC 3.1.- (Endodeoxyribonucleases); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx612


  6 / 1095 MEDLINE  
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[PMID]:28846925
[Au] Autor:Wu L; Uldahl KB; Chen F; Benasutti H; Logvinski D; Vu V; Banda NK; Peng X; Simberg D; Moghimi SM
[Ad] Endereço:Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, People's Republic of China.
[Ti] Título:Interaction of extremophilic archaeal viruses with human and mouse complement system and viral biodistribution in mice.
[So] Source:Mol Immunol;90:273-279, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Archaeal viruses offer exceptional biophysical properties for modification and exploration of their potential in bionanotechnology, bioengineering and nanotherapeutic developments. However, the interaction of archaeal viruses with elements of the innate immune system has not been explored, which is a necessary prerequisite if their potential for biomedical applications to be realized. Here we show complement activation through lectin (via direct binding of MBL/MASPs) and alternative pathways by two extremophilic archaeal viruses (Sulfolobus monocaudavirus 1 and Sulfolobus spindle-shaped virus 2) in human serum. We further show some differences in initiation of complement activation pathways between these viruses. Since, Sulfolobus monocaudavirus 1 was capable of directly triggering the alternative pathway, we also demonstrate that the complement regulator factor H has no affinity for the viral surface, but factor H deposition is purely C3-dependent. This suggests that unlike some virulent pathogens Sulfolobus monocaudavirus 1 does not acquire factor H for protection. Complement activation with Sulfolobus monocaudavirus 1 also proceeds in murine sera through MBL-A/C as well as factor D-dependent manner, but C3 deficiency has no overall effect on viral clearance by organs of the reticuloendothelial system on intravenous injection. However, splenic deposition was significantly higher in C3 knockout animals compared with the corresponding wild type mice. We discuss the potential application of these viruses in biomedicine in relation to their complement activating properties.
[Mh] Termos MeSH primário: Vírus de Archaea/imunologia
Ativação do Complemento/imunologia
Via Alternativa do Complemento/imunologia
Imunidade Inata/imunologia
[Mh] Termos MeSH secundário: Adulto
Animais
Complemento C3/genética
Complemento C3/imunologia
Fator H do Complemento/imunologia
Extremófilos/imunologia
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microscopia Eletrônica de Transmissão
Sulfolobus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Complement C3); 80295-65-4 (Complement Factor H)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  7 / 1095 MEDLINE  
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[PMID]:28681456
[Au] Autor:Stiefler-Jensen D; Schwarz-Linnet T; de Lichtenberg C; Nguyen TTTN; Rand KD; Huang L; She Q; Teilum K
[Ad] Endereço:Archaea Centre, Department of Biology, University of Copenhagen, København, Denmark.
[Ti] Título:The extraordinary thermal stability of EstA from S. islandicus is independent of post translational modifications.
[So] Source:Protein Sci;26(9):1819-1827, 2017 Sep.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enzymes from thermophilic and hyper-thermophilic organisms have an intrinsic high stability. Understanding the mechanisms behind their high stability will be important knowledge for the engineering of novel enzymes with high stability. Lysine methylation of proteins is prevalent in Sulfolobus, a genus of hyperthermophilic and acidophilic archaea. Both unspecific and temperature dependent lysine methylations are seen, but the significance of this post-translational modification has not been investigated. Here, we test the effect of eliminating in vivo lysine methylation on the stability of an esterase (EstA). The enzyme was purified from the native host S. islandicus as well as expressed as a recombinant protein in E. coli, a mesophilic host that does not code for any machinery for in vivo lysine methylation. We find that lysine mono methylation indeed has a positive effect on the stability of EstA, but the effect is small. The effect of the lysine methylation on protein stability is secondary to that of protein expression in E. coli, as the E. coli recombinant enzyme is compromised both on stability and activity. We conclude that these differences are not attributed to any covalent difference between the protein expressed in hyperthermophilic versus mesophilic hosts.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Hidrolases de Éster Carboxílico/química
Hidrolases de Éster Carboxílico/metabolismo
Sulfolobus/enzimologia
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Hidrolases de Éster Carboxílico/genética
Escherichia coli/genética
Lisina/metabolismo
Metilação
Processamento de Proteína Pós-Traducional
Estabilidade Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sulfolobus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Recombinant Proteins); EC 3.1.1.- (Carboxylic Ester Hydrolases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3220


  8 / 1095 MEDLINE  
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[PMID]:28647366
[Au] Autor:Yan Z; Yuan Z; Ni J; Gu L; Shen Y
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Rd., Jinan, 250100, PR China.
[Ti] Título:Crystal structure of the crenarchaeal ExoIII AP endonuclease SisExoIII reveals a conserved disulfide bond endowing the protein with thermostability.
[So] Source:Biochem Biophys Res Commun;490(3):774-779, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AP endonuclease recognizes and cleaves apurinic/apyrimidinic (AP) sites and plays a critical role in base excision repair. Many ExoIII and EndoIV family AP endonucleases have been characterized both biochemically and structurally in Eukaryote and Bacteria. However, relatively fewer have been studied in Euryarchaeota and there is no such report on an AP endonuclease from Crenarchaeota. Here we report, for the first time, the crystal structure of a crenarchaeal ExoIII AP endonuclease, SisExoIII, from Sulfolobus islandicus REY15A. SisExoIII comprises a two-layer core formed by 10 ß-sheets and a shell formed by 9 surrounding α-helices. A disulfide bond connecting ß8 and ß9 is formed by Cys142 and Cys215. This intra-molecular linkage is conserved among crenarchaeal ExoIII homologs and site-directed mutagenesis revealed that it endows the protein with thermostability, however, disruption of the disulfide bond only has a slight effect on the AP endonuclease activity. We also observed that several key residues within the catalytic center including conserved Glu35 and Asn9 show different conformation compared with known ExoIII proteins and form various intra-molecular salt bridges. The protein possesses three putative DNA binding loops with higher flexibility and hydrophobicity than those of ExoIIIs from other organisms. These features may result in low AP endonuclease activity and defect of exonuclease activity of SisExoIII. The study has deepened our understanding in the structural basis of crenarchaeal ExoIII catalysis and clarified a role of the disulfide bond in maintaining protein thermostability.
[Mh] Termos MeSH primário: DNA Liase (Sítios Apurínicos ou Apirimidínicos)/química
Exodesoxirribonucleases/química
Sulfolobus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Estabilidade Enzimática
Modelos Moleculares
Conformação Proteica
Alinhamento de Sequência
Sulfolobus/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.2 (exodeoxyribonuclease III); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170626
[St] Status:MEDLINE


  9 / 1095 MEDLINE  
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[PMID]:28625421
[Au] Autor:Gaglione R; Pirone L; Farina B; Fusco S; Smaldone G; Aulitto M; Dell'Olmo E; Roscetto E; Del Gatto A; Fattorusso R; Notomista E; Zaccaro L; Arciello A; Pedone E; Contursi P
[Ad] Endereço:Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.
[Ti] Título:Insights into the anticancer properties of the first antimicrobial peptide from Archaea.
[So] Source:Biochim Biophys Acta;1861(9):2155-2164, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The peptide VLL-28, identified in the sequence of an archaeal protein, the transcription factor Stf76 from Sulfolobus islandicus, was previously identified and characterized as an antimicrobial peptide, possessing a broad-spectrum antibacterial activity. METHODS: Through a combined approach of NMR and Circular Dichroism spectroscopy, Dynamic Light Scattering, confocal microscopy and cell viability assays, the interaction of VLL-28 with the membranes of both parental and malignant cell lines has been characterized and peptide mechanism of action has been studied. RESULTS: It is here demonstrated that VLL-28 selectively exerts cytotoxic activity against murine and human tumor cells. By means of structural methodologies, VLL-28 interaction with the membranes has been proven and the binding residues have been identified. Confocal microscopy data show that VLL-28 is internalized only into tumor cells. Finally, it is shown that cell death is mainly caused by a time-dependent activation of apoptotic pathways. CONCLUSIONS: VLL-28, deriving from the archaeal kingdom, is here found to be endowed with selective cytotoxic activity towards both murine and human cancer cells and consequently can be classified as an ACP. GENERAL SIGNIFICANCE: VLL-28 represents the first ACP identified in an archaeal microorganism, exerting a trans-kingdom activity.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/farmacologia
Antineoplásicos/farmacologia
Sulfolobus/química
[Mh] Termos MeSH secundário: Animais
Peptídeos Catiônicos Antimicrobianos/química
Antineoplásicos/química
Células 3T3 BALB
Morte Celular/efeitos dos fármacos
Membrana Celular/efeitos dos fármacos
Dicroísmo Circular
Seres Humanos
Camundongos
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Antineoplastic Agents)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE


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[PMID]:28424284
[Au] Autor:Liu Y; Ishino S; Ishino Y; Pehau-Arnaudet G; Krupovic M; Prangishvili D
[Ad] Endereço:Department of Microbiology, BMGE, Institut Pasteur, Paris, France.
[Ti] Título:A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea.
[So] Source:J Virol;91(13), 2017 Jul 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Encapsidation of genetic material into polyhedral particles is one of the most common structural solutions employed by viruses infecting hosts in all three domains of life. Here, we describe a new virus of hyperthermophilic archaea, polyhedral virus 1 (SPV1), which condenses its circular double-stranded DNA genome in a manner not previously observed for other known viruses. The genome complexed with virion proteins is wound up sinusoidally into a spherical coil which is surrounded by an envelope and further encased by an outer polyhedral capsid apparently composed of the 20-kDa virion protein. Lipids selectively acquired from the pool of host lipids are integral constituents of the virion. None of the major virion proteins of SPV1 show similarity to structural proteins of known viruses. However, minor structural proteins, which are predicted to mediate host recognition, are shared with other hyperthermophilic archaeal viruses infecting members of the order The SPV1 genome consists of 20,222 bp and contains 45 open reading frames, only one-fifth of which could be functionally annotated. Viruses infecting hyperthermophilic archaea display a remarkable morphological diversity, often presenting architectural solutions not employed by known viruses of bacteria and eukaryotes. Here we present the isolation and characterization of polyhedral virus 1, which condenses its genome into a unique spherical coil. Due to the original genomic and architectural features of SPV1, the virus should be considered a representative of a new viral family, "Portogloboviridae."
[Mh] Termos MeSH primário: Vírus de DNA/classificação
Vírus de DNA/isolamento & purificação
Sulfolobus/virologia
Estruturas Virais
[Mh] Termos MeSH secundário: Vírus de DNA/genética
Vírus de DNA/ultraestrutura
Ordem dos Genes
Genoma Viral
Microscopia Eletrônica
Fases de Leitura Aberta
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
Proteínas Virais/genética
Vírion/química
Vírion/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Proteins)
[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:170421
[St] Status:MEDLINE



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