TY - JOUR. T1 - DNA helicase E and DNA polymerase ∈ functionally interact for displacement synthesis. AU - Turchi, John. AU - Siegal, Gregg. AU - Bambara, Robert A.. PY - 1992. Y1 - 1992. N2 - A functional interaction between DNA helicase E and DNA polymerase ∈ from calf thymus has been detected which results in the extension of an upstream 3′ OH through a downstream primer to the end of a synthetic template. DNA synthesis resulting in full-length extension products was dependent on the addition of DNA helicase E and hydrolysis of ATP, suggesting that displacement of the downstream primer was required. Identical reactions using DNA polymerases α and δ in place of DNA polymerase ∈ showed no full-length products dependent on helicase E, indicating that polymerases α and δ were incapable of functionally interacting with the helicase. The reaction leading to full-length extension products was time dependent and dependent on the concentration of added polymerase ∈ and helicase E. ...
Excellgen Brahma-related Gene 1 protein, wild type, BRG1, SMARCA4 [RP-22] - Product Name Brahma-related Gene 1, BRG1, SMARCA4 Size 5,000 U Description The wild type human brahma-related gene 1 (Brg1) encodes a protein of 1,647 amino acids that contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription regulation (1-3). BRG1 is an essential component of the SWI/SNF chromatin remodeling complexes
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Escherichia coli DNA helicase II plays a specific role in the methyl‐directed mismatch repair and nucleotide excision repair pathways (Caron et al., 1985; Husain et al., 1985; Lahue et al., 1989), a less defined role in recombination (Horii and Clark, 1973; Arthur and Lloyd, 1980; Feinstein and Low, 1986; Schellhorn and Low, 1991; Mendonca et al., 1993, 1995; Morel et al., 1993) and possibly replication (Taucher‐Scholz and Hoffman‐Berling, 1983; Washburn and Kushner, 1991; George et al., 1994; Brosh and Matson, 1995). We used the yeast two‐hybrid system to search for interacting protein partners that might direct the involvement of helicase II in one or more of these processes. The two‐hybrid screen revealed an interaction between helicase II and MutL, an essential component for methyl‐directed mismatch repair and, according to a recent report, a factor in transcription‐coupled nucleotide excision repair (Mellon and Champe, 1996).. Deletion analysis demonstrated that the ...
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
BioMed Research International is a peer-reviewed, Open Access journal that publishes original research articles, review articles, and clinical studies covering a wide range of subjects in life sciences and medicine. The journal is divided into 55 subject areas.
DNA helicases are a diverse group of enzymes that separate the two strands of duplex DNA. Using the free energy derived from the hydrolysis of a 5ʹ nucleoside triphosphate, generally ATP, the helicase catalyzes the unwinding of duplex DNA to yield single-stranded DNA (ssDNA), a process that is required in replication, transcription, recombination, and repair. Thus, helicases are involved in essentially all metabolic pathways that require the separation of duplex DNA (Brosh 2013; Khan et al. 2015).. Helicases exhibit a diversity of structure and mechanism that may be related to the often unique and specialized roles that these enzymes can play in the cell (Brosh 2013; Daley et al. 2013). Importantly, distinct helicases can interact with specific DNA substrates. For example, during repair of DNA damage, different helicases often act within particular pathways and on unique DNA intermediates that are generated as repair progresses, such as Holliday junctions (HJs) or displacement loops (D-loops). ...
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Frye, Stephan Alfons; Balasingham, Seetha; Beyene, Getachew Tesfaye; Homberset, Håvard; Namouchi, Amine & Tonjum, Tone (2016). Meningococcal DNA binding and unwinding proteins. Show summary Background: DNA helicases are a ubiquitous group of enzymes that use the energy of nucleoside triphosphate (dNTP) hydrolysis to catalyze the separation of double-stranded DNA (dsDNA). Helicases are involved in essentially every step in DNA metabolism, including replication, DNA repair, recombination, transcription, Holliday junction movement, and displacement of proteins from DNA. We investigated the DNA helicases RecG and DinG from Neisseria meningitidis (NmRecG and NmDinG) and their roles during genotoxic stress, including DNA damage. These helicases belong to superfamily 2, are ATP dependent and exert 5′to 3′ directionality. Our aim was to define the potential roles of NmRecG and NmDinG in DNA repair, recombination and replication (3R). Methods and results: Cell lysates from Nm wildtype and recG and ...
Our group studies the process of homologous recombination. We focus on the DNA motor protein complexes or DNA nano-machines responsible for driving this process. These machines are frequently coupled to, or powered by, DNA helicases. DNA helicases are ubiquitous enzymes whose primary function is to unwind DNA duplexes into their component single strands, a process that is coupled to the hydrolysis of nucleoside 5-triposphates. Our work is aimed at understanding the biochemical mechanism of DNA helicases and how these mechanisms contribute to and are adapted to the processes of recombination and DNA repair.. To see how DNA nano-machines put it all together, we use state-of-the-art single molecule techniques to visualize in real time, the dynamic properties of DNA nan-machines that are lost in the averaging process using conventional ensemble assays. Single molecule manipulation and observation techniques provide an unparalleled and dramatic means to study biological reactions. The two techniques ...
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DNA is a helical, double-stranded molecule that bears the genetic code. During the replication of DNA, its two strands are separated from each other resulting in a configuration called the replication fork. The replication fork is comprised of two prongs wherein each prong is the single strand of DNA. The replication fork results from the work of the helicases. Helicases are enzymes that are used by living organisms to separate the strands of nucleic acids, and in this case, the double-stranded DNA. Helicases do so by breaking the hydrogen bonds that hold the two strands together. Helicases are able to do this by utilizing energy from the hydrolysis of nucleoside triphosphates (e.g. ATPs). Apart from DNA replication, helicases are also used in transcription, translation, recombination, DNA repair, and ribosome biogenesis. DNA helicases were first discovered and isolated in E.coli in 1976.1 ...
ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Figure 6. Translocation Mechanism and Directional Polarity(A) Schematic of a Rho translocation cycle in which six ATP molecules are hydrolyzed to move six nucleotides of RNA. Helicase subunits are illustrated as colored spheres. RNA is shown as a chain of white spheres spiraling out of the plane of the paper. Protein-RNA contacts are indicated by lines connecting the protein and RNA spheres; the black RNA sphere serves as a reference point and moves toward the viewer as the boxed red subunit transitions through six steps in the translocation cycle. A yellow star represents activation of the allosteric network that likely promotes hydrolysis. See also Movies S3-S6.(B) Schematics of Rho and E1 (chains A-F) illustrating their respective sequential ATP hydrolysis directions. Protein subunits are colored as inFigure 1. Nucleic acid phosphates observed in the structures are illustrated as bold orange circles, with the incoming phosphate shown as a dashed orange circle. Rectangles represent the two ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
DNA helicase. Molecular model of a helicase molecule from the SV40 virus. Helicases are enzymes that separate the two strands of the DNA double helix, by breaking the hydrogen bonds between nucleotide bases. Separation of the strands is needed for replication, and therefore this protein is vital for the ability of the virus to infect host cells. - Stock Image F006/9426
RuvBL1 helicase enzyme, molecular model. Helicases are enzymes that carry out several roles, primarily separating the two strands of the DNA (deoxyribonucleic acid) double helix, by breaking the hydrogen bonds between nucleotide bases. RuvBL1 plays important roles in the c-Myc and Wnt signalling pathways that are vital to chromatin remodelling, and transcriptional and developmental regulation. It also plays roles in DNA repair and apoptosis (programmed cell death). Here, it forms a cyclic hexamer, with six monomers highlighted by the colours used here. - Stock Image C015/4304
7 MemProtMD simulations of ATP-dependent helicase activity in a lipid bilayer at both coarse-grained and atomistic respresentation, including both file download and analysis. Classification based on GO GO:0008026.
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Abstract : To trigger transcription termination, the ring-shaped RNA-DNA helicase Rho from Escherichia coli chases the RNA polymerase along the nascent transcript, starting from a single-stranded C-rich Rut (Rho utilization) loading site. In some instances, a small hairpin structure divides harmlessly the C-rich loading region into two smaller Rut subsites, best exemplified by the tR1 terminator from phage lambda. Here, we show that the Rho helicase can also elude a RNA structural block located far downstream from the single-stranded C-rich region but upstream from a reporter RNA-DNA hybrid.. ...
ATPase and helicase activities of Brr2 mutants. (a) Locations of residues corresponding to brr2-1 (E610G) and brr2-R1107A on the Hel308 structure (PDB ID 2P6R 2
Rabbit anti LGP2 (N-Terminal) antibody recognizes human Probable ATP-dependent helicase LGP2 (LGP2), also known as DHX58, a 768aa cytoplas
K14439 SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 [EC:3.6.4.12 ...
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A plethora of mutations in chromatin regulators in diverse human cancers is emerging, attesting to the pivotal role of chromatin dynamics in tumorigenesis. A recurrent theme is inactivation of the chromodomain helicase DNA-binding (CHD) family of proteins-ATP-dependent chromatin remodelers that govern the cellular machinerys access to DNA, thereby controlling fundamental processes, including transcription, proliferation, and DNA damage repair. This review highlights what is currently known about how genetic and epigenetic perturbation of CHD proteins and the pathways that they regulate set the stage for cancer, providing new insight for designing more effective anti-cancer therapies.. ...
TY - JOUR. T1 - DNA-RNA helicase activity of RAD3 protein of Saccharomyces cerevisiae. AU - Bailly, Véronique. AU - Sung, Patrick. AU - Prakash, Louise. AU - Prakash, Satya. PY - 1991. Y1 - 1991. N2 - The RAD3 gene of Saccharomyces cerevisiae is required for excision repair of UV-damaged DNA and is essential for cell viability. The RAD3 protein exhibits a remarkable degree of sequence homology to the human excision repair protein ERCC2. The RAD3 protein is a single-stranded DNA-dependent ATPase and a DNA helicase capable of denaturing long regions of duplex DNA. Here, we demonstrate that RAD3 also possesses a potent DNA-RNA helicase activity similar in efficiency to its DNA helicase activity. The rad3 Arg-48 mutant protein, which binds but does not hydrolyze ATP, lacks the DNA-RNA unwinding activity, indicating a dependence on ATP hydrolysis. RAD3 does not show any RNA-dependent NTPase activity and, as expected, does not unwind duplex RNA. This observation suggests that RAD3 translocates on DNA ...
The S. cerevisiae yeast transcriptional activator SNF2/SWI2 protein enzymes consist of two alpha/beta-lobes similar to SF2 helicases exons 7 and 8 that activates homeotic genes designated BRG1 (brm/SWI2-related gene-1) (BAF) complexes locus: 19p13.2, [§§], express two homologs of the SWI2 subunit. A conserved ATP binding site residue in BRG1 display conventional chromatin-remodeling activity and genomic Left-handed Z-DNA stability (the helicase-like screw motion of DNA motor proteins of human SWI/SNF along the active site.) and enhanced the DNA strand-exchange activity, whereas transcription requires, in addition, an activation domain intergenic solitary (LTRs) long terminal repeat subunits of Pol IVb are targeted, to successfully culminate the repair, indicate a communication and compensation between Brm and Brg-1. BRCA1 can directly interact with the BRG1. BRCA1 is associated with a SWI/SNF-related complex SMARCA4 and the tumor suppressor SMARCB1 the hSNF5/INI1 gene, allowing access to ...
Silva AP, Ryan DP, Galanty Y, Low JK, Vandevenne M, Jackson SP, Mackay JP. Journal of Biological Chemistry 291, 924-938. Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA damage responses through its N-terminal region in a poly(ADP-ribose) polymerase dependent manner. We have identified and determined the structure of a stable domain (CHD4-N) in this N-terminal region.
XPB helicase is an integral part of transcription factor TFIIH, required for both transcription initiation and nucleotide excision repair (NER). Along with the XPD helicase, XPB plays a crucial but only partly understood role in defining and extending the DNA repair bubble around lesions in NER. Archaea encode clear homologues of XPB and XPD, and structural studies of these proteins have yielded key insights relevant to the eukaryal system. Here we show that archaeal XPB functions with a structure-specific nuclease, Bax1, as a helicase-nuclease machine that unwinds and cleaves model NER substrates. DNA bubbles are extended by XPB and cleaved by Bax1 at a position equivalent to that cut by the XPG nuclease in eukaryal NER. The helicase activity of archaeal XPB is dependent on the conserved Thumb domain, which may act as the helix breaker. The N-terminal damage recognition domain of XPB is shown to be crucial for XPB-Bax1 activity and may be unique to the archaea. These findings have implications ...
Although Pif1 helicase family members are highly similar throughout their helicase domains, their amino termini are diverse. For example, the two S. cerevisiae Pif1 family members, Pif1p and Rrm3p, are 60% similar within their ∼450-amino-acid helicase domain but have no significant similarity within their ∼250-amino-acid amino termini (Figure 1). Since a truncated Rrm3p that lacks the first 194 amino acids of the protein has ATPase and 5′ to 3′ DNA helicase activity, the amino terminus is not required for in vitro activity (Ivessa et al. 2002). This article examines the in vivo function of the Rrm3p amino terminus. We constructed a series of alleles that lacked all or part of the amino terminus of Rrm3p (Figure 2A) and tested their ability to support fork progression at three Rrm3p-dependent loci, to suppress activation of DNA checkpoints, and to maintain viability in the absence of checkpoint and repair genes.. By each of these in vivo assays, the amino terminus of Rrm3p was essential ...
PO debconf template translation of kismet # Copyright (C) 2013 THE kismetS COPYRIGHT HOLDER # This file is distributed under the same license as the kismet package. # José de Figueiredo ,[email protected],, 2013. # msgid msgstr Project-Id-Version: kismet\n Report-Msgid-Bugs-To: [email protected]\n POT-Creation-Date: 2012-12-15 14:36+0100\n PO-Revision-Date: 2013-07-15 08:19-0300\n Last-Translator: José de Figueiredo ,[email protected],\n Language-Team: Brazilian Portuguese ,[email protected],\n Language: \n MIME-Version: 1.0\n Content-Type: text/plain; charset=UTF-8\n Content-Transfer-Encoding: 8bit\n #. Type: boolean #. Description #: ../kismet.templates:2001 msgid Install Kismet \setuid root\? msgstr Instalar o Kismet com \setuid root\? #. Type: boolean #. Description #: ../kismet.templates:2001 msgid Kismet needs root privileges for some of its functions. However, running it as root (\sudo kismet\) is ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Manganese atom in PDB 3dkx: Crystal Structure of the Replication Initiator Protein Encoded on Plasmid PMV158 (Repb), Trigonal Form, to 2.7 Ang Resolution
Helicase loader protein (gp59) was found to form a hexamer on forked DNA and the presence of gp32 and gp41 increased the stability of the formed complex.
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Structures of this kind are often considered to occur in RNA, but if they also occur in single-stranded DNA, it raises interesting questions. If a gene has an energetically stable strands-apart configuration, getting the strands of duplex B-form DNA to separate might not be so hard. But more to the point, getting the self-annealing gene to come back together again as duplex DNA will require significant energy input. In molecular genetics, were accustomed to the idea of duplex DNA requiring help from an ATP-dependent helicase to "open up" (unwind) the double helix in preparation for replication or transcription. The above diagram suggests that the problem isnt "opening up" a gene; the greater problem may be bringing the strands together again after theyve assumed a stable strands-apart secondary structure. Theres a substantial energy barrier to be overcome before the above structure can be relaxed into randomly coiling DNA ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumorsuppressor protein RB1/RB. Alternatively spliced transcript variants encoding distinct isoforms have been reported ...
The RecQ helicase family is a group of highly conserved DNA unwinding enzymes critical in guarding genome stability in all kingdoms of life. Human RecQ homologs...
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Complete information for CHD8 gene (Protein Coding), Chromodomain Helicase DNA Binding Protein 8, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for CHD9 gene (Protein Coding), Chromodomain Helicase DNA Binding Protein 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The binary distribution of Mcm2‐7 across the genome prompted us to investigate genomic features that may be associated with the broad regions of high or low Mcm2‐7 levels along the chromosome. The Mcm2‐7 localization pattern relative to annotated genomic features suggested that Mcm2‐7 may be displaced by actively transcribed genes (Fig 5A). To quantitatively assess the Mcm2‐7 distribution relative to transcription units, we generated histograms of Mcm2‐7 enrichment for transcribed and non‐transcribed genes (Fig 5B) and found a bimodal pattern of Mcm2‐7 enrichment. Specifically, active genes had no or very little Mcm2‐7 signal, whereas inactive or non‐transcribed genes exhibited an elevated Mcm2‐7 signal (P , 1.02 × 10−257; t = 40.16). We also considered that the bimodal distribution of Mcm2‐7 enrichment between active and inactive genes might be due to the activation of early origins that are enriched near actively transcribed genes. However, we found that the bimodal ...
CHD1 - CHD1 (untagged)-Human chromodomain helicase DNA binding protein 1 (CHD1) available for purchase from OriGene - Your Gene Company.
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Tran PLT, Pohl TJ, Chen CF, Chan A, Pott S, Zakian VA. PIF1 family DNA helicases suppress R-loop mediated genome instability at tRNA genes. Nat Commun. 2017 04 21; 8:15025 ...
3 direction only. In this schematic, the replication fork (RF) is shown as opening to the right. On the lower leading strand, synthesis is continuous because extension of a single RNA primer occurs without interruption into the replication fork as it continues to open to the right. On the upper lagging strand, synthesis is discontinuous, since new RNA primers must be added as opening of the replication fork continues to expose new template. This produces a series of disconnected Okazaki fragments ...
Background The protein encoded by this gene is a member of the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Members of this family have helicase and ATPase activities and are thought to...
This gene encodes a lymphoid-specific helicase. Other helicases function in processes involving DNA strand separation, including replication, repair, recombination, and transcription. This protein is thought to be involved with cellular proliferation and may play a role in leukemogenesis. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jan 2014] ...