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[PMID]:27523731
[Au] Autor:Bezsudnova EY; Stekhanova TN; Suplatov DA; Mardanov AV; Ravin NV; Popov VO
[Ad] Endereço:A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, Bld. 2, 119071, Moscow, Russian Federation. Electronic address: eubez@inbi.ras.ru.
[Ti] Título:Experimental and computational studies on the unusual substrate specificity of branched-chain amino acid aminotransferase from Thermoproteus uzoniensis.
[So] Source:Arch Biochem Biophys;607:27-36, 2016 Oct 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PLP-Dependent fold-type IV branched-chain amino acid aminotransferases (BCATs) from archaea have so far been poorly characterized. A new BCAT from the hyperthermophilic archaeon Thermoproteus uzoniensis (TUZN1299) has been studied. TUZN1299 was found to be highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, l-methionine, l-threonine, l-homoserine, l-glutamine, as well as toward 2-oxobutyrate and keto analogs of BCAAs, whereas l-glutamate and α-ketoglutarate were not converted in the overall reaction. According to stopped-flow experiments, the enzyme showed the highest specificity to BCAAs and their keto analogs. In order to explain the molecular mechanism of the unusual specificity of TUZN1299, bioinformatic analysis was implemented to identify the subfamily-specific positions in the aminotransferase class IV superfamily of enzymes. The role of the selected residues in binding of various ligands in the active site was further studied using molecular modeling. The results indicate that Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for α-ketoglutarate and l-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket. The likely functional roles of TUZN1299 in cellular metabolism - in the synthesis and degradation of BCAAs - are discussed.
[Mh] Termos MeSH primário: Aminoácidos de Cadeia Ramificada/química
Biologia Computacional/métodos
Thermoproteus/enzimologia
Transaminases/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Simulação por Computador
Cristalografia por Raios X
Glutamina/química
Concentração de Íons de Hidrogênio
Cinética
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); 0RH81L854J (Glutamine); EC 2.6.1.- (Transaminases); EC 2.6.1.42 (branched-chain-amino-acid transaminase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE


  2 / 38 MEDLINE  
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[PMID]:26872794
[Au] Autor:Boyko KM; Stekhanova TN; Nikolaeva AY; Mardanov AV; Rakitin AL; Ravin NV; Bezsudnova EY; Popov VO
[Ad] Endereço:A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, Moscow, 119071, Russian Federation. kmb@inbi.ras.ru.
[Ti] Título:First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines.
[So] Source:Extremophiles;20(2):215-25, 2016 Mar.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The gene TUZN1299 from the genome of the hyperthermophilic archaeon Thermoproteus uzoniensis encoding a new 32.8 kDa branched-chain amino acid aminotransferase (BCAT) was expressed in Escherichia coli. The recombinant protein TUZN1299 was purified to homogeneity in the PLP-bound form. TUZN1299 was active towards branched-chain amino acids (L-Val, L-Leu, L-Ile) and showed low but detectable activity toward (R)-alpha-methylbenzylamine. The enzyme exhibits high-temperature optimum, thermal stability, and tolerance to organic solvents. The structure of an archaeal BCAT called TUZN1299 was solved for the first time (at 2.0 Å resolution). TUZN1299 has a typical BCAT type IV fold, and the organization of its active site is similar to that of bacterial BCATs. However, there are some differences in the amino acid composition of the active site.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Thermoproteus/enzimologia
Transaminases/química
[Mh] Termos MeSH secundário: Aminas/química
Aminas/metabolismo
Aminoácidos de Cadeia Ramificada/química
Aminoácidos de Cadeia Ramificada/metabolismo
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Estabilidade Enzimática
Especificidade por Substrato
Transaminases/genética
Transaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amines); 0 (Amino Acids, Branched-Chain); 0 (Archaeal Proteins); EC 2.6.1.- (Transaminases); EC 2.6.1.42 (branched-chain-amino-acid transaminase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:160214
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-016-0816-z


  3 / 38 MEDLINE  
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[PMID]:26514828
[Au] Autor:Krupovic M; Cvirkaite-Krupovic V; Prangishvili D; Koonin EV
[Ad] Endereço:Department of Microbiology, Unité Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, 75015, France. krupovic@pasteur.fr.
[Ti] Título:Evolution of an archaeal virus nucleocapsid protein from the CRISPR-associated Cas4 nuclease.
[So] Source:Biol Direct;10:65, 2015 Oct 29.
[Is] ISSN:1745-6150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many proteins of viruses infecting hyperthermophilic Crenarchaeota have no detectable homologs in current databases, hampering our understanding of viral evolution. We used sensitive database search methods and structural modeling to show that a nucleocapsid protein (TP1) of Thermoproteus tenax virus 1 (TTV1) is a derivative of the Cas4 nuclease, a component of the CRISPR-Cas adaptive immunity system that is encoded also by several archaeal viruses. In TTV1, the Cas4 gene was split into two, with the N-terminal portion becoming TP1, and lost some of the catalytic amino acid residues, apparently resulting in the inactivation of the nuclease. To our knowledge, this is the first described case of exaptation of an enzyme for a virus capsid protein function.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Endonucleases/genética
Evolução Molecular
Lipothrixviridae/enzimologia
Lipothrixviridae/genética
Proteínas do Nucleocapsídeo/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Sistemas CRISPR-Cas
Endonucleases/metabolismo
Proteínas do Nucleocapsídeo/metabolismo
Thermoproteus/genética
Thermoproteus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Nucleocapsid Proteins); EC 3.1.- (Endonucleases)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151031
[St] Status:MEDLINE
[do] DOI:10.1186/s13062-015-0093-2


  4 / 38 MEDLINE  
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[PMID]:26499493
[Au] Autor:Plagens A; Daume M; Wiegel J; Randau L
[Ad] Endereço:Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.
[Ti] Título:Circularization restores signal recognition particle RNA functionality in Thermoproteus.
[So] Source:Elife;4, 2015 Oct 24.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Signal recognition particles (SRPs) are universal ribonucleoprotein complexes found in all three domains of life that direct the cellular traffic and secretion of proteins. These complexes consist of SRP proteins and a single, highly structured SRP RNA. Canonical SRP RNA genes have not been identified for some Thermoproteus species even though they contain SRP19 and SRP54 proteins. Here, we show that genome rearrangement events in Thermoproteus tenax created a permuted SRP RNA gene. The 5'- and 3'-termini of this SRP RNA are located close to a functionally important loop present in all known SRP RNAs. RNA-Seq analyses revealed that these termini are ligated together to generate circular SRP RNA molecules that can bind to SRP19 and SRP54. The circularization site is processed by the tRNA splicing endonuclease. This moonlighting activity of the tRNA splicing machinery permits the permutation of the SRP RNA and creates highly stable and functional circular RNA molecules.
[Mh] Termos MeSH primário: RNA/metabolismo
Partícula de Reconhecimento de Sinal/metabolismo
Thermoproteus/genética
Thermoproteus/metabolismo
[Mh] Termos MeSH secundário: RNA/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
Partícula de Reconhecimento de Sinal/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, circular); 0 (Signal Recognition Particle); 63231-63-0 (RNA); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160202
[Lr] Data última revisão:
160202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151027
[St] Status:MEDLINE


  5 / 38 MEDLINE  
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[PMID]:25981464
[Au] Autor:Plagens A; Randau L
[Ad] Endereço:Prokaryotic Small RNA Biology, Max-Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043, Marburg, Germany, andre.plagens@mpi-marburg.mpg.de.
[Ti] Título:In Vitro Co-reconstitution of Cas Protein Complexes.
[So] Source:Methods Mol Biol;1311:23-33, 2015.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CRISPR-Cas systems employ diverse and often multimeric CRISPR-associated (Cas) protein effector complexes to mediate antiviral defense. The elucidation of the mechanistic details and the protein interaction partners requires production of recombinant Cas proteins. However, these proteins are often produced as inactive inclusion bodies. Here, we present a detailed protocol for the isolation and purification of insoluble Cas proteins. Guidelines for their solubilization via co-reconstitution strategies and procedures to upscale the production of soluble multimeric Cas protein complexes are provided.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/isolamento & purificação
Proteínas Associadas a CRISPR/química
Proteínas Associadas a CRISPR/isolamento & purificação
[Mh] Termos MeSH secundário: Corpos de Inclusão/química
Multimerização Proteica
Redobramento de Proteína
Estrutura Quaternária de Proteína
Solubilidade
Thermoproteus/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (CRISPR-Associated Proteins)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150518
[Lr] Data última revisão:
150518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150519
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-2687-9_2


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[PMID]:25933622
[Au] Autor:June Yim K; Seon Song H; Choi JS; Woon Roh S
[Ad] Endereço:1​ Biological Disaster Analysis Group, Korea Basic Science Institute, Daejeon 305-806, Republic of Korea 2​ Department of Biology, Jeju National University, Jeju 690-756, Republic of Korea.
[Ti] Título:Thermoproteus thermophilus sp. nov., a hyperthermophilic crenarchaeon isolated from solfataric soil.
[So] Source:Int J Syst Evol Microbiol;65(8):2507-10, 2015 Aug.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A hyperthermophilic crenarchaeon, designated strain CBA1502T, was isolated from volcanic soil in the Mayon volcano in the Philippines. The 16S rRNA gene sequence of strain CBA1502T was most closely related to that of Thermoproteus uzoniensis DSM 5263T (99.2% similarity) and Thermoproteus tenax Kra 1T (99.0%). The organism grew at 75-90°C and pH 4.0-6.0 and in the presence of 0-0.5% (w/v) NaCl, with optimal growth at 85°C and pH 5.0. Strain CBA1502T utilized d-arabinose, beef extract, Casamino acids, formate, fumarate, peptone, pyruvate, trimethylamine and yeast extract as energy substrates, and d-arabinose, formate, pyruvate and yeast extract as carbon sources. Fumarate, sulfate, sulfur and thiosulfate functioned as electron acceptors, but not ferric chloride, nitrate, malate or oxidized glutathione. DNA-DNA hybridization studies showed that there was less than 46.1% relatedness between strain CBA1502T and other members of the genus Thermoproteus. The DNA G+C content of strain CBA1502T was 62.0 mol%. We conclude that, according to its phylogenetic, phenotypic and genotypic characteristics, strain CBA1502T represents a novel species of the genus Thermoproteus, and propose the name Thermoproteus thermophilus sp. nov., with the type strain CBA1502T ( = ATCC BAA-2416T = JCM 17229T).
[Mh] Termos MeSH primário: Filogenia
Microbiologia do Solo
Thermoproteus/classificação
[Mh] Termos MeSH secundário: Composição de Bases
DNA Arqueal/genética
Dados de Sequência Molecular
Hibridização de Ácido Nucleico
Filipinas
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Thermoproteus/genética
Thermoproteus/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Archaeal); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150902
[Lr] Data última revisão:
150902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150503
[St] Status:MEDLINE
[do] DOI:10.1099/ijs.0.000293


  7 / 38 MEDLINE  
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[PMID]:25746627
[Au] Autor:Aiba H; Nishiya Y; Azuma M; Yokooji Y; Atomi H; Imanaka T
[Ad] Endereço:a Institute of Biotechnology , TOYOBO CO., LTD. , Tsuruga , Japan.
[Ti] Título:Characterization of a thermostable glucose dehydrogenase with strict substrate specificity from a hyperthermophilic archaeon Thermoproteus sp. GDH-1.
[So] Source:Biosci Biotechnol Biochem;79(7):1094-102, 2015.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A hyperthermophilic archaeon was isolated from a terrestrial hot spring on Kodakara Island, Japan and designated as Thermoproteus sp. glucose dehydrogenase (GDH-1). Cell extracts from cells grown in medium supplemented with glucose exhibited NAD(P)-dependent glucose dehydrogenase activity. The enzyme (TgGDH) was purified and found to display a strict preference for D-glucose. The gene was cloned and expressed in Escherichia coli, resulting in the production of a soluble and active protein. Recombinant TgGDH displayed extremely high thermostability and an optimal temperature higher than 85 °C, in addition to its strict specificity for D-glucose. Despite its thermophilic nature, TgGDH still exhibited activity at 25 °C. We confirmed that the enzyme could be applied for glucose measurements at ambient temperatures, suggesting a potential of the enzyme for use in measurements in blood samples.
[Mh] Termos MeSH primário: Glucose 1-Desidrogenase/química
Glucose 1-Desidrogenase/metabolismo
Thermoproteus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Clonagem Molecular
Estabilidade Enzimática
Escherichia coli/genética
Glucose/metabolismo
Glucose 1-Desidrogenase/genética
Japão
Cinética
Dados de Sequência Molecular
RNA Ribossômico 16S
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Solubilidade
Especificidade por Substrato
Temperatura Ambiente
Thermoproteus/genética
Thermoproteus/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (RNA, Ribosomal, 16S); 0 (Recombinant Proteins); EC 1.1.1.47 (Glucose 1-Dehydrogenase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150703
[Lr] Data última revisão:
150703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150310
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2015.1018120


  8 / 38 MEDLINE  
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[PMID]:25148031
[Au] Autor:Daume M; Plagens A; Randau L
[Ad] Endereço:Prokaryotic Small RNA Biology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.
[Ti] Título:DNA binding properties of the small cascade subunit Csa5.
[So] Source:PLoS One;9(8):e105716, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CRISPR-Cas systems provide immunity against viral attacks in archaeal and bacterial cells. Type I systems employ a Cas protein complex termed Cascade, which utilizes small CRISPR RNAs to detect and degrade the exogenic DNA. A small sequence motif, the PAM, marks the foreign substrates. Previously, a recombinant type I-A Cascade complex from the archaeon Thermoproteus tenax was shown to target and degrade DNA in vitro, dependent on a native PAM sequence. Here, we present the biochemical analysis of the small subunit, Csa5, of this Cascade complex. T. tenax Csa5 preferentially bound ssDNA and mutants that showed decreased ssDNA-binding and reduced Cascade-mediated DNA cleavage were identified. Csa5 oligomerization prevented DNA binding. Specific recognition of the PAM sequence was not observed. Phylogenetic analyses identified Csa5 as a universal member of type I-A systems and revealed three distinct groups. A potential role of Csa5 in R-loop stabilization is discussed.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Sistemas CRISPR-Cas/fisiologia
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas/fisiologia
DNA Arqueal/metabolismo
DNA de Cadeia Simples/metabolismo
Thermoproteus/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
DNA Arqueal/genética
DNA de Cadeia Simples/genética
Thermoproteus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (DNA, Archaeal); 0 (DNA, Single-Stranded)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:140823
[Lr] Data última revisão:
140823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0105716


  9 / 38 MEDLINE  
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[PMID]:25139066
[Au] Autor:Urbanek BL; Wing DC; Haislop KS; Hamel CJ; Kalscheuer R; Woodruff PJ; Swarts BM
[Ad] Endereço:Department of Chemistry, Central Michigan University, Mount Pleasant, MI 48859 (USA).
[Ti] Título:Chemoenzymatic synthesis of trehalose analogues: rapid access to chemical probes for investigating mycobacteria.
[So] Source:Chembiochem;15(14):2066-70, 2014 Sep 22.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Trehalose analogues are emerging as valuable tools for investigating Mycobacterium tuberculosis, but progress in this area is slow due to the difficulty in synthesizing these compounds. Here, we report a chemoenzymatic synthesis of trehalose analogues that employs the heat-stable enzyme trehalose synthase (TreT) from the hyperthermophile Thermoproteus tenax. By using TreT, various trehalose analogues were prepared quickly (1 h) in high yield (up to >99 % by HPLC) in a single step from readily available glucose analogues. To demonstrate the utility of this method in mycobacteria research, we performed a simple "one-pot metabolic labeling" experiment that accomplished probe synthesis, metabolic labeling, and imaging of M. smegmatis in a single day with only TreT and commercially available materials.
[Mh] Termos MeSH primário: Glucosiltransferases/metabolismo
Infecções por Mycobacterium/microbiologia
Mycobacterium/citologia
Mycobacterium/metabolismo
Thermoproteus/enzimologia
Trealose/análogos & derivados
Trealose/metabolismo
[Mh] Termos MeSH secundário: Química Click
Seres Humanos
Microscopia de Fluorescência
Mycobacterium smegmatis/citologia
Mycobacterium smegmatis/metabolismo
Mycobacterium tuberculosis/citologia
Mycobacterium tuberculosis/metabolismo
Trealose/síntese química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (trehalose synthase)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140912
[Lr] Data última revisão:
140912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140821
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201402288


  10 / 38 MEDLINE  
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[PMID]:24500198
[Au] Autor:Plagens A; Tripp V; Daume M; Sharma K; Klingl A; Hrle A; Conti E; Urlaub H; Randau L
[Ad] Endereço:Prokaryotic Small RNA Biology Group, Max Planck Institute for Terrestrial Microbiology, D-35043 Marburg, Germany, Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany, Cell Biology and LOEWE Research Centre for Synthetic Microbiology, Philipps-Universität Marburg, D-35043 Marburg, Germany and Department of Structural Cell Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
[Ti] Título:In vitro assembly and activity of an archaeal CRISPR-Cas type I-A Cascade interference complex.
[So] Source:Nucleic Acids Res;42(8):5125-38, 2014 Apr.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)-CRISPR-associated (Cas) systems of type I use a Cas ribonucleoprotein complex for antiviral defense (Cascade) to mediate the targeting and degradation of foreign DNA. To address molecular features of the archaeal type I-A Cascade interference mechanism, we established the in vitro assembly of the Thermoproteus tenax Cascade from six recombinant Cas proteins, synthetic CRISPR RNAs (crRNAs) and target DNA fragments. RNA-Seq analyses revealed the processing pattern of crRNAs from seven T. tenax CRISPR arrays. Synthetic crRNA transcripts were matured by hammerhead ribozyme cleavage. The assembly of type I-A Cascade indicates that Cas3' and Cas3'' are an integral part of the complex, and the interference activity was shown to be dependent on the crRNA and the matching target DNA. The reconstituted Cascade was used to identify sequence motifs that are required for efficient DNA degradation and to investigate the role of the subunits Cas7 and Cas3'' in the interplay with other Cascade subunits.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Proteínas Associadas a CRISPR/metabolismo
Sistemas CRISPR-Cas
Desoxirribonucleases/metabolismo
[Mh] Termos MeSH secundário: Clivagem do DNA
DNA Arqueal/metabolismo
DNA de Cadeia Simples/metabolismo
Exodesoxirribonucleases/metabolismo
Processamento Pós-Transcricional do RNA
RNA Arqueal/química
RNA Arqueal/metabolismo
Thermoproteus/enzimologia
Thermoproteus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (CRISPR-Associated Proteins); 0 (DNA, Archaeal); 0 (DNA, Single-Stranded); 0 (RNA, Archaeal); EC 3.1.- (Deoxyribonucleases); EC 3.1.- (Exodeoxyribonucleases)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:150515
[Lr] Data última revisão:
150515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140207
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gku120



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