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  1 / 1203 MEDLINE  
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[PMID]:28743747
[Au] Autor:Bermek O; Weller SK; Griffith JD
[Ad] Endereço:From the Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7295 and oya_bermek@med.unc.edu.
[Ti] Título:The UL8 subunit of the helicase-primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.
[So] Source:J Biol Chem;292(38):15611-15621, 2017 09 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During lytic infection, herpes simplex virus (HSV) DNA is replicated by a mechanism involving DNA recombination. For instance, replication of the HSV-1 genome produces X- and Y-branched structures, reminiscent of recombination intermediates. HSV-1's replication machinery includes a trimeric helicase-primase composed of helicase (UL5) and primase (UL52) subunits and a third subunit, UL8. UL8 has been reported to stimulate the helicase and primase activities of the complex in the presence of ICP8, an HSV-1 protein that functions as an annealase, a protein that binds complementary single-stranded DNA (ssDNA) and facilitates its annealing to duplex DNA. UL8 also influences the intracellular localization of the UL5/UL52 subunits, but UL8's catalytic activities are not known. In this study we used a combination of biochemical techniques and transmission electron microscopy. First, we report that UL8 alone forms protein filaments in solution. Moreover, we also found that UL8 binds to ssDNAs >50-nucletides long and promotes the annealing of complementary ssDNA to generate highly branched duplex DNA structures. Finally, UL8 has a very high affinity for replication fork structures containing a gap in the lagging strand as short as 15 nucleotides, suggesting that UL8 may aid in directing or loading the trimeric complex onto a replication fork. The properties of UL8 uncovered here suggest that UL8 may be involved in the generation of the X- and Y-branched structures that are the hallmarks of HSV replication.
[Mh] Termos MeSH primário: DNA Helicases/metabolismo
DNA Primase/metabolismo
Replicação do DNA
Herpesvirus Humano 1/enzimologia
Herpesvirus Humano 1/genética
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
DNA de Cadeia Simples/biossíntese
DNA de Cadeia Simples/química
DNA de Cadeia Simples/metabolismo
Herpesvirus Humano 1/ultraestrutura
Peso Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA, Single-Stranded); 0 (Viral Proteins); EC 2.7.7.- (DNA Primase); EC 3.1.- (helicase-primase, Human herpesvirus 1); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.799064


  2 / 1203 MEDLINE  
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[PMID]:28977480
[Au] Autor:Peralta-Castro A; Baruch-Torres N; Brieba LG
[Ad] Endereço:Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Apartado Postal 629, Irapuato, Guanajuato, CP 36821, México.
[Ti] Título:Plant organellar DNA primase-helicase synthesizes RNA primers for organellar DNA polymerases using a unique recognition sequence.
[So] Source:Nucleic Acids Res;45(18):10764-10774, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:DNA primases recognize single-stranded DNA (ssDNA) sequences to synthesize RNA primers during lagging-strand replication. Arabidopsis thaliana encodes an ortholog of the DNA primase-helicase from bacteriophage T7, dubbed AtTwinkle, that localizes in chloroplasts and mitochondria. Herein, we report that AtTwinkle synthesizes RNA primers from a 5'-(G/C)GGA-3' template sequence. Within this sequence, the underlined nucleotides are cryptic, meaning that they are essential for template recognition but are not instructional during RNA synthesis. Thus, in contrast to all primases characterized to date, the sequence recognized by AtTwinkle requires two nucleotides (5'-GA-3') as a cryptic element. The divergent zinc finger binding domain (ZBD) of the primase module of AtTwinkle may be responsible for template sequence recognition. During oligoribonucleotide synthesis, AtTwinkle shows a strong preference for rCTP as its initial ribonucleotide and a moderate preference for rGMP or rCMP incorporation during elongation. RNA products synthetized by AtTwinkle are efficiently used as primers for plant organellar DNA polymerases. In sum, our data strongly suggest that AtTwinkle primes organellar DNA polymerases during lagging strand synthesis in plant mitochondria and chloroplast following a primase-mediated mechanism. This mechanism contrasts to lagging-strand DNA replication in metazoan mitochondria, in which transcripts synthesized by mitochondrial RNA polymerase prime mitochondrial DNA polymerase γ.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
DNA Helicases/metabolismo
DNA Primase/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Enzimas Multifuncionais/metabolismo
RNA/biossíntese
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Sequência de Bases
Proteínas de Cloroplastos/química
Proteínas de Cloroplastos/genética
Proteínas de Cloroplastos/metabolismo
Sequência Conservada
DNA Helicases/química
DNA Helicases/genética
DNA Primase/química
DNA Primase/genética
DNA de Cadeia Simples/química
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Enzimas Multifuncionais/química
Enzimas Multifuncionais/genética
Ligação Proteica
Ribonucleotídeos/biossíntese
Moldes Genéticos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Chloroplast Proteins); 0 (DNA, Single-Stranded); 0 (Mitochondrial Proteins); 0 (Multifunctional Enzymes); 0 (RNA primers); 0 (Ribonucleotides); 0 (Twinkle protein, Arabidopsis); 63231-63-0 (RNA); EC 2.7.7.- (DNA Primase); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 3.6.4.- (DNA Helicases)
[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/gkx745


  3 / 1203 MEDLINE  
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[PMID]:28934486
[Au] Autor:Ganduri S; Lue NF
[Ad] Endereço:Department of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medical College, New York, NY 10065, USA.
[Ti] Título:STN1-POLA2 interaction provides a basis for primase-pol α stimulation by human STN1.
[So] Source:Nucleic Acids Res;45(16):9455-9466, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The CST (CTC1-STN1-TEN1) complex mediates critical functions in maintaining telomere DNA and overcoming genome-wide replication stress. A conserved biochemical function of the CST complex is its primase-Pol α (PP) stimulatory activity. In this report, we demonstrate the ability of purified human STN1 alone to promote PP activity in vitro. We show that this regulation is mediated primarily by the N-terminal OB fold of STN1, but does not require the DNA-binding activity of this domain. Rather, we observed a strong correlation between the PP-stimulatory activity of STN1 variants and their abilities to bind POLA2. Remarkably, the main binding target of STN1 in POLA2 is the latter's central OB fold domain. In the substrate-free structure of PP, this domain is positioned so as to block nucleic acid entry to the Pol α active site. Thus the STN1-POLA2 interaction may promote the necessary conformational change for nucleic acid delivery to Pol α and subsequent DNA synthesis. A disease-causing mutation in human STN1 engenders a selective defect in POLA2-binding and PP stimulation, indicating that these activities are critical for the in vivo function of STN1. Our findings have implications for the molecular mechanisms of PP, STN1 and STN1-related molecular pathology.
[Mh] Termos MeSH primário: DNA Polimerase I/metabolismo
DNA Primase/metabolismo
Proteínas de Ligação a Telômeros/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
DNA/metabolismo
DNA Polimerase I/química
DNA Polimerase I/genética
DNA Primase/química
DNA Primase/genética
Seres Humanos
Mutação Puntual
Domínios Proteicos
Subunidades Proteicas
Proteínas de Ligação a Telômeros/química
Proteínas de Ligação a Telômeros/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Stn1 protein, human); 0 (Telomere-Binding Proteins); 9007-49-2 (DNA); EC 2.7.7.- (DNA Polymerase I); EC 2.7.7.- (DNA Primase); EC 2.7.7.- (DNA polymerase alpha-primase); EC 2.7.7.- (POLA2 protein, human)
[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/gkx621


  4 / 1203 MEDLINE  
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[PMID]:28911121
[Au] Autor:Agudo R; Calvo PA; Martínez-Jiménez MI; Blanco L
[Ad] Endereço:Centro de Biología Molecular 'Severo Ochoa' (CSIC-UAM), Cantoblanco, E-28049 Madrid, Spain.
[Ti] Título:Engineering human PrimPol into an efficient RNA-dependent-DNA primase/polymerase.
[So] Source:Nucleic Acids Res;45(15):9046-9058, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have developed a straightforward fluorometric assay to measure primase-polymerase activity of human PrimPol (HsPrimPol). The sensitivity of this procedure uncovered a novel RNA-dependent DNA priming-polymerization activity (RdDP) of this enzyme. In an attempt to enhance HsPrimPol RdDP activity, we constructed a smart mutant library guided by prior sequence-function analysis, and tested this library in an adapted screening platform of our fluorometric assay. After screening less than 500 variants, we found a specific HsPrimPol mutant, Y89R, which displays 10-fold higher RdDP activity than the wild-type enzyme. The improvement of RdDP activity in the Y89R variant was due mainly to an increased in the stabilization of the preternary complex (protein:template:incoming nucleotide), a specific step preceding dimer formation. Finally, in support of the biotechnological potential of PrimPol as a DNA primer maker during reverse transcription, mutant Y89R HsPrimPol rendered up to 17-fold more DNA than with random hexamer primers.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Bioensaio
DNA Primase/genética
DNA Polimerase Dirigida por DNA/genética
Enzimas Multifuncionais/genética
Engenharia de Proteínas/métodos
DNA Polimerase Dirigida por RNA/genética
RNA/genética
[Mh] Termos MeSH secundário: Arginina/química
Arginina/metabolismo
Clonagem Molecular
DNA Primase/metabolismo
Primers do DNA/síntese química
Primers do DNA/química
DNA Polimerase Dirigida por DNA/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Corantes Fluorescentes/química
Fluorometria/métodos
Expressão Gênica
Biblioteca Gênica
Seres Humanos
Enzimas Multifuncionais/metabolismo
Mutação
Oligonucleotídeos/química
Oligonucleotídeos/metabolismo
Compostos Orgânicos/química
Ligação Proteica
Multimerização Proteica
RNA/metabolismo
DNA Polimerase Dirigida por RNA/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa/métodos
Tirosina/química
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Primers); 0 (Fluorescent Dyes); 0 (Multifunctional Enzymes); 0 (Oligonucleotides); 0 (Organic Chemicals); 163795-75-3 (SYBR Green I); 42HK56048U (Tyrosine); 63231-63-0 (RNA); 94ZLA3W45F (Arginine); EC 2.7.7.- (DNA Primase); EC 2.7.7.- (PrimPol protein, human); EC 2.7.7.49 (RNA-Directed DNA Polymerase); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[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/gkx633


  5 / 1203 MEDLINE  
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[PMID]:28902865
[Au] Autor:Boldinova EO; Stojkovic G; Khairullin R; Wanrooij S; Makarova AV
[Ad] Endereço:Institute of Molecular Genetics of Russian Academy of Sciences, Kurchatov sq. 2, Moscow, Russia.
[Ti] Título:Optimization of the expression, purification and polymerase activity reaction conditions of recombinant human PrimPol.
[So] Source:PLoS One;12(9):e0184489, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human PrimPol is a DNA primase/polymerase involved in DNA damage tolerance and prevents nuclear genome instability. PrimPol is also localized to the mitochondria, but its precise function in mitochondrial DNA maintenance has remained elusive. PrimPol works both as a translesion (TLS) polymerase and as the primase that restarts DNA replication after a lesion. However, the observed biochemical activities of PrimPol vary considerably between studies as a result of different reaction conditions used. To reveal the effects of reaction composition on PrimPol DNA polymerase activity, we tested the polymerase activity in the presence of various buffer agents, salt concentrations, pH values and metal cofactors. Additionally, the enzyme stability was analyzed under various conditions. We demonstrate that the reaction buffer with pH 6-6.5, low salt concentrations and 3 mM Mg2+ or 0.3-3 mM Mn2+ cofactor ions supports the highest DNA polymerase activity of human PrimPol in vitro. The DNA polymerase activity of PrimPol was found to be stable after multiple freeze-thaw cycles and prolonged protein incubation on ice. However, rapid heat-inactivation of the enzyme was observed at 37ºC. We also for the first time describe the purification of human PrimPol from a human cell line and compare the benefits of this approach to the expression in Escherichia coli and in Saccharomyces cerevisiae cells. Our results show that active PrimPol can be purified from E. coli and human suspension cell line in high quantities and that the activity of the purified enzyme is similar in both expression systems. Conversely, the yield of full-length protein expressed in S. cerevisiae was considerably lower and this system is therefore not recommended for expression of full-length recombinant human PrimPol.
[Mh] Termos MeSH primário: DNA Primase/genética
DNA Primase/isolamento & purificação
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/isolamento & purificação
Enzimas Multifuncionais/genética
Enzimas Multifuncionais/isolamento & purificação
Reação em Cadeia da Polimerase/normas
[Mh] Termos MeSH secundário: Calibragem
Células Cultivadas
DNA Primase/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Células HEK293
Seres Humanos
Engenharia Metabólica/normas
Enzimas Multifuncionais/metabolismo
Organismos Geneticamente Modificados
Reação em Cadeia da Polimerase/métodos
Estabilidade Proteica
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multifunctional Enzymes); 0 (Recombinant Proteins); EC 2.7.7.- (DNA Primase); EC 2.7.7.- (PrimPol protein, human); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184489


  6 / 1203 MEDLINE  
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[PMID]:28729485
[Au] Autor:O'Brien E; Holt ME; Thompson MK; Salay LE; Ehlinger AC; Chazin WJ; Barton JK
[Ad] Endereço:Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
[Ti] Título:Response to Comments on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
[So] Source:Science;357(6348), 2017 07 21.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Baranovskiy and Pellegrini argue that, based on structural data, the path for charge transfer through the [4Fe4S] domain of primase is not feasible. Our manuscript presents electrochemical data directly showing charge transport through DNA to the [4Fe4S] cluster of a primase p58C construct and a reversible switch in the DNA-bound signal with oxidation/reduction, which is inhibited by mutation of three tyrosine residues. Although the dispositions of tyrosines differ in different constructs, all are within range for microsecond electron transfer.
[Mh] Termos MeSH primário: DNA Primase/química
Oxirredução
[Mh] Termos MeSH secundário: Transporte Biológico
DNA
Transporte de Elétrons
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.7.7.- (DNA Primase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


  7 / 1203 MEDLINE  
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[PMID]:28729486
[Au] Autor:Pellegrini L
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Cambridge, UK.
[Ti] Título:Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
[So] Source:Science;357(6348), 2017 07 21.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:O'Brien (Research Article, 24 February 2017, eaag1789) report that the iron-sulfur cluster of primase has a redox role in enzyme activity. Their analysis is based on a partially misfolded structure of the iron-sulfur cluster domain of primase. In the correctly folded structure, two of the three tyrosines putatively involved in electron transfer, Y345 and Y347, contact the RNA/DNA helix, providing an alternative explanation for the data of O'Brien .
[Mh] Termos MeSH primário: DNA Primase/química
Proteínas com Ferro-Enxofre/química
[Mh] Termos MeSH secundário: DNA
Seres Humanos
Oxirredução
Enxofre/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 70FD1KFU70 (Sulfur); 9007-49-2 (DNA); EC 2.7.7.- (DNA Primase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


  8 / 1203 MEDLINE  
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[PMID]:28729484
[Au] Autor:Baranovskiy AG; Babayeva ND; Zhang Y; Blanco L; Pavlov YI; Tahirov TH
[Ad] Endereço:Eppley Institute for Research in Cancer and Allied Diseases, Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.
[Ti] Título:Comment on "The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport".
[So] Source:Science;357(6348), 2017 07 21.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:O'Brien (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.
[Mh] Termos MeSH primário: DNA Primase/genética
Oxirredução
[Mh] Termos MeSH secundário: Transporte Biológico
DNA
Seres Humanos
Proteínas com Ferro-Enxofre/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; COMMENT
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 9007-49-2 (DNA); EC 2.7.7.- (DNA Primase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


  9 / 1203 MEDLINE  
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[PMID]:28575448
[Au] Autor:Seco EM; Ayora S
[Ad] Endereço:Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.
[Ti] Título:Bacillus subtilis DNA polymerases, PolC and DnaE, are required for both leading and lagging strand synthesis in SPP1 origin-dependent DNA replication.
[So] Source:Nucleic Acids Res;45(14):8302-8313, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Firmicutes have two distinct replicative DNA polymerases, the PolC leading strand polymerase, and PolC and DnaE synthesizing the lagging strand. We have reconstituted in vitro Bacillus subtilis bacteriophage SPP1 θ-type DNA replication, which initiates unidirectionally at oriL. With this system we show that DnaE is not only restricted to lagging strand synthesis as previously suggested. DnaG primase and DnaE polymerase are required for initiation of DNA replication on both strands. DnaE and DnaG synthesize in concert a hybrid RNA/DNA 'initiation primer' on both leading and lagging strands at the SPP1 oriL region, as it does the eukaryotic Pol α complex. DnaE, as a RNA-primed DNA polymerase, extends this initial primer in a reaction modulated by DnaG and one single-strand binding protein (SSB, SsbA or G36P), and hands off the initiation primer to PolC, a DNA-primed DNA polymerase. Then, PolC, stimulated by DnaG and the SSBs, performs the bulk of DNA chain elongation at both leading and lagging strands. Overall, these modulations by the SSBs and DnaG may contribute to the mechanism of polymerase switch at Firmicutes replisomes.
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Proteínas de Bactérias/metabolismo
Bacteriófagos/genética
DNA Polimerase III/metabolismo
Replicação do DNA
DNA Polimerase Dirigida por DNA/metabolismo
[Mh] Termos MeSH secundário: Bacillus subtilis/virologia
Bacteriófagos/metabolismo
Sequência de Bases
DNA Primase/metabolismo
DNA de Cadeia Simples/metabolismo
DNA Viral/genética
DNA Viral/metabolismo
Proteínas de Ligação a DNA/metabolismo
Eletroforese em Gel de Ágar
Ligação Proteica
Origem de Replicação/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Single-Stranded); 0 (DNA, Viral); 0 (DNA-Binding Proteins); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (DNA Primase); EC 2.7.7.- (DNA polymerase III, alpha subunit); EC 2.7.7.- (PolC protein, bacteria); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx493


  10 / 1203 MEDLINE  
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[PMID]:28520934
[Au] Autor:Märtens B; Hou L; Amman F; Wolfinger MT; Evguenieva-Hackenberg E; Bläsi U
[Ad] Endereço:Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, Center of Molecular Biology, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, 1030 Vienna, Austria.
[Ti] Título:The SmAP1/2 proteins of the crenarchaeon Sulfolobus solfataricus interact with the exosome and stimulate A-rich tailing of transcripts.
[So] Source:Nucleic Acids Res;45(13):7938-7949, 2017 Jul 27.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The conserved Sm and Sm-like proteins are involved in different aspects of RNA metabolism. Here, we explored the interactome of SmAP1 and SmAP2 of the crenarchaeon Sulfolobus solfataricus (Sso) to shed light on their physiological function(s). Both, SmAP1 and SmAP2 co-purified with several proteins involved in RNA-processing/modification, translation and protein turnover as well as with components of the exosome involved in 3΄ to 5΄ degradation of RNA. In follow-up studies a direct interaction with the poly(A) binding and accessory exosomal subunit DnaG was demonstrated. Moreover, elevated levels of both SmAPs resulted in increased abundance of the soluble exosome fraction, suggesting that they affect the subcellular localization of the exosome in the cell. The increased solubility of the exosome was accompanied by augmented levels of RNAs with A-rich tails that were further characterized using RNASeq. Hence, the observation that the Sso SmAPs impact on the activity of the exosome revealed a hitherto unrecognized function of SmAPs in archaea.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
RNA Arqueal/metabolismo
Sulfolobus solfataricus/metabolismo
[Mh] Termos MeSH secundário: Sequência Rica em At
Proteínas Arqueais/genética
DNA Primase/genética
DNA Primase/metabolismo
Exossomos/genética
Exossomos/metabolismo
Estabilidade de RNA
RNA Arqueal/química
RNA Arqueal/genética
Solubilidade
Sulfolobus solfataricus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (RNA, Archaeal); 0 (SmAP protein, Pyrobaculum aerophilum); EC 2.7.7.- (DNA Primase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx437



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