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Готові списки джерел за темами / DnaB helicase / Статті в журналах

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Статті в журналах з теми "DnaB helicase"

Автор: Grafiati

Опубліковано: 4 березня 2024

Оновлено: 31 липня 2025

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1

Titok, Marina, Catherine Suski, Bérengère Dalmais, S. Dusko Ehrlich, and Laurent Jannière. "The replicative polymerases PolC and DnaE are required for theta replication of the Bacillus subtilis plasmid pBS72." Microbiology 152, no. 5 (2006): 1471–78. http://dx.doi.org/10.1099/mic.0.28693-0.

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Plasmids are the tools of choice for studying bacterial functions involved in DNA maintenance. Here a genetic study on the replication of a novel, low-copy-number, Bacillus subtilis plasmid, pBS72, is reported. The results show that two plasmid elements, the initiator protein RepA and an iteron-containing origin, and at least nine host-encoded replication proteins, the primosomal proteins DnaB, DnaC, DnaD, DnaG and DnaI, the DNA polymerases DnaE and PolC, and the polymerase cofactors DnaN and DnaX, are required for pBS72 replication. On the contrary, the cellular initiators DnaA and PriA, the

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2

Hayashi, Chihiro, Erika Miyazaki, Shogo Ozaki, Yoshito Abe, and Tsutomu Katayama. "DnaB helicase is recruited to the replication initiation complex via binding of DnaA domain I to the lateral surface of the DnaB N-terminal domain." Journal of Biological Chemistry 295, no. 32 (2020): 11131–43. http://dx.doi.org/10.1074/jbc.ra120.014235.

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The DNA replication protein DnaA in Escherichia coli constructs higher-order complexes on the origin, oriC, to unwind this region. DnaB helicase is loaded onto unwound oriC via interactions with the DnaC loader and the DnaA complex. The DnaB–DnaC complex is recruited to the DnaA complex via stable binding of DnaB to DnaA domain I. The DnaB–DnaC complex is then directed to unwound oriC via a weak interaction between DnaB and DnaA domain III. Previously, we showed that Phe46 in DnaA domain I binds to DnaB. Here, we searched for the DnaA domain I–binding site in DnaB. The DnaB L160A variant was i

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3

Bazin, Alexandre, Mickaël Cherrier, and Laurent Terradot. "Structural insights into DNA replication initiation in Helicobacter pylori." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1632. http://dx.doi.org/10.1107/s2053273314083673.

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In Gram-negative bacteria, opening of DNA double strand during replication is performed by the replicative helicase DnaB. This protein allows for replication fork elongation by unwinding DNA and interacting with DnaG primase. DnaB is composed of two domains: an N-terminal domain (NTD) and a C-terminal domain (CTD) connected by a flexible linker. The protein forms two-tiered hexamers composed of a NTD-ring and a CTD-ring. In Escherichia coli, the initiator protein DnaA binds to the origin of replication oriC and induces the opening of a AT-rich region. The replicative helicase DnaB is then load

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4

Huang, Yen-Hua, and Cheng-Yang Huang. "Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT." BioMed Research International 2014 (2014): 1–14. http://dx.doi.org/10.1155/2014/195162.

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Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome inEscherichia coliis composed of PriA helicase, PriB, PriC, DnaT, DnaC, DnaB helicase, and DnaG primase. The assembly of the protein complexes within the forked DNA responsible for reloading the replicative DnaB helicase anywhere on the chromosome for genome duplication requires the coordination of transient biomolecular interactions. Over

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5

Sharma, Dhakaram Pangeni, Ramachandran Vijayan, Syed Arif Abdul Rehman, and Samudrala Gourinath. "Structural insights into the interaction of helicase and primase in Mycobacterium tuberculosis." Biochemical Journal 475, no. 21 (2018): 3493–509. http://dx.doi.org/10.1042/bcj20180673.

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The helicase–primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain of primase (DnaG) and N-terminal domain of helicase (DnaB). To understand the functional conservation despite the low sequence homology of the DnaB-binding domains of DnaGs of eubacteria, we determined the crystal structure of the helicase-binding domain of DnaG from Mycobacterium tuberculosis (MtDnaG-CTD) and did so to a resolution of 1.58 Å. We observed the overall structure of MtDnaG-CTD to consist of two subdomains, the N-terminal globular region (GR) and the C

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6

Nagata, Koji, Akitoshi Okada, Jun Ohtsuka, et al. "Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding." Journal of Biochemistry 167, no. 1 (2019): 1–14. http://dx.doi.org/10.1093/jb/mvz087.

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Abstract Loading the bacterial replicative helicase DnaB onto DNA requires a specific loader protein, DnaC/DnaI, which creates the loading-competent state by opening the DnaB hexameric ring. To understand the molecular mechanism by which DnaC/DnaI opens the DnaB ring, we solved 3.1-Å co-crystal structure of the interaction domains of Escherichia coli DnaB–DnaC. The structure reveals that one N-terminal domain (NTD) of DnaC interacts with both the linker helix of a DnaB molecule and the C-terminal domain (CTD) of the adjacent DnaB molecule by forming a three α-helix bundle, which fixes the rela

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7

Donate, L. E., M. Bárcena, O. Llorca, N. Dixon, and J. M. Carazo. "Quaternary Polymorphism in Helicases and the DnaB.DnaC Complex." Microscopy and Microanalysis 6, S2 (2000): 272–73. http://dx.doi.org/10.1017/s1431927600033857.

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Strand separation in double stranded DNA is achieved in vivo by a class of enzymes called helicases in a process fuelled by hydrolysis of nucleoside triphosphates. DnaB is the major replicative helicase in E.coli. For chromosomal replication to initiate, DnaB needs to interact with a partner protein, namely DnaC, which after properly loading DnaB onto the DNA template at the origin of replication is subsequently released from the complex. DnaB turns to be functionally active as a helicase only after DnaC has been released from the complex. The native DnaB is a homohexamer of molecular weight 3

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8

Saveson, Catherine J., and Susan T. Lovett. "Enhanced Deletion Formation by Aberrant DNA Replication in Escherichia coli." Genetics 146, no. 2 (1997): 457–70. http://dx.doi.org/10.1093/genetics/146.2.457.

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Repeated genes and sequences are prone to genetic rearrangements including deletions. We have investigated deletion formation in Escherichia coli strains mutant for various replication functions. Deletion was selected between 787 base pair tandem repeats carried either on a ColE1-derived plasmid or on the E. coli chromosome. Only mutations in functions associated with DNA Polymerase III elevated deletion rates in our assays. Especially large increases were observed in strains mutant in dnaQ the ϵ editing subunit of Pol III, and dnuB, the replication fork helicase. Mutations in several other fu

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9

Odegrip, Richard, Stephan Schoen, Elisabeth Haggård-Ljungquist, Kyusung Park, and Dhruba K. Chattoraj. "The Interaction of Bacteriophage P2 B Protein with Escherichia coli DnaB Helicase." Journal of Virology 74, no. 9 (2000): 4057–63. http://dx.doi.org/10.1128/jvi.74.9.4057-4063.2000.

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ABSTRACT Bacteriophage P2 requires several host proteins for lytic replication, including helicase DnaB but not the helicase loader, DnaC. Some genetic studies have suggested that the loading is done by a phage-encoded protein, P2 B. However, a P2 minichromosome containing only the P2 initiator gene A and a marker gene can be established as a plasmid without requiring the P2 B gene. Here we demonstrate that P2 B associates with DnaB. This was done by using the yeast two-hybrid system in vivo and was confirmed in vitro, where 35S-labeled P2 B bound specifically to DnaB adsorbed to Q Sepharose b

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10

Spinks, Richard R., Lisanne M. Spenkelink, Sarah A. Stratmann, et al. "DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies." Nucleic Acids Research 49, no. 12 (2021): 6804–16. http://dx.doi.org/10.1093/nar/gkab493.

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Abstract In Escherichia coli, the DnaB helicase forms the basis for the assembly of the DNA replication complex. The stability of DnaB at the replication fork is likely important for successful replication initiation and progression. Single-molecule experiments have significantly changed the classical model of highly stable replication machines by showing that components exchange with free molecules from the environment. However, due to technical limitations, accurate assessments of DnaB stability in the context of replication are lacking. Using in vitro fluorescence single-molecule imaging, w

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11

BISWAS, Subhasis B., Stephen FLOWERS, and Esther E. BISWAS-FISS. "Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli." Biochemical Journal 379, no. 3 (2004): 553–62. http://dx.doi.org/10.1042/bj20031255.

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In this study, we have presented the first report of Escherichia coli DnaC protein binding to ssDNA (single stranded DNA) in an apparent hexameric form. DnaC protein transfers DnaB helicase onto a nascent chromosomal DNA replication fork at oriC, the origin of E. coli DNA replication. In eukaryotes, Cdc6 protein may play a similar role in the DNA helicase loading in the replication fork during replication initiation at the origin. We have analysed the DNA-binding properties of DnaC protein and a quantitative analysis of the nucleotide regulation of DnaC–DNA and DnaC–DnaB interactions using flu

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12

Felczak, Magdalena M., Sundari Chodavarapu, and Jon M. Kaguni. "DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase." Journal of Biological Chemistry 292, no. 51 (2017): 20871–82. http://dx.doi.org/10.1074/jbc.m117.807644.

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13

Syeda, Aisha H., Adam J. M. Wollman, Alex L. Hargreaves, et al. "Single-molecule live cell imaging of Rep reveals the dynamic interplay between an accessory replicative helicase and the replisome." Nucleic Acids Research 47, no. 12 (2019): 6287–98. http://dx.doi.org/10.1093/nar/gkz298.

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Abstract DNA replication must cope with nucleoprotein barriers that impair efficient replisome translocation. Biochemical and genetic studies indicate accessory helicases play essential roles in replication in the presence of nucleoprotein barriers, but how they operate inside the cell is unclear. With high-speed single-molecule microscopy we observed genomically-encoded fluorescent constructs of the accessory helicase Rep and core replisome protein DnaQ in live Escherichia coli cells. We demonstrate that Rep colocalizes with 70% of replication forks, with a hexameric stoichiometry, indicating

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14

Soni, Rajesh K., Parul Mehra, Gauranga Mukhopadhyay, and Suman Kumar Dhar. "Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo." Biochemical Journal 389, no. 2 (2005): 541–48. http://dx.doi.org/10.1042/bj20050062.

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Анотація:

In Escherichia coli, DnaC is essential for loading DnaB helicase at oriC (the origin of chromosomal DNA replication). The question arises as to whether this model can be generalized to other species, since many eubacterial species fail to possess dnaC in their genomes. Previously, we have reported the characterization of HpDnaB (Helicobacter pylori DnaB) both in vitro and in vivo. Interestingly, H. pylori does not have a DnaC homologue. Using two different E. coli dnaC (EcdnaC) temperature-sensitive mutant strains, we report here the complementation of EcDnaC function by HpDnaB in vivo. These

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15

Thirlway, Jenny, and Panos Soultanas. "In the Bacillus stearothermophilus DnaB-DnaG Complex, the Activities of the Two Proteins Are Modulated by Distinct but Overlapping Networks of Residues." Journal of Bacteriology 188, no. 4 (2006): 1534–39. http://dx.doi.org/10.1128/jb.188.4.1534-1539.2006.

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ABSTRACTWe demonstrate the primase activity ofBacillus stearothermophilusDnaG and show that it initiates at 3′-ATC-5′ and 3′-ATT-5′ sites synthesizing primers that are 22 or 23 nucleotides long. In the presence of the helicase DnaB the size distribution of primers is different, and a range of additional smaller primers are also synthesized. Nine residues from the N- and C-terminal domains of DnaB, as well as its linker region, have been reported previously to affect this interaction. InBacillus stearothermophilusonly three residues from the linker region (I119 and I125) and the N-terminal doma

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16

Cargemel, Claire, Stéphanie Marsin, Magali Noiray, et al. "The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders." Acta Crystallographica Section D Structural Biology 79, no. 2 (2023): 177–87. http://dx.doi.org/10.1107/s2059798323000281.

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During the initiation step of bacterial genome replication, replicative helicases depend on specialized proteins for their loading onto oriC. DnaC and DnaI were the first loaders to be characterized. However, most bacteria do not contain any of these genes, which are domesticated phage elements that have replaced the ancestral and unrelated loader gene dciA several times during evolution. To understand how DciA assists the loading of DnaB, the crystal structure of the complex from Vibrio cholerae was determined, in which two VcDciA molecules interact with a dimer of VcDnaB without changing its

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17

Behrmann, Megan S., Himasha M. Perera, Joy M. Hoang, et al. "Targeted chromosomal Escherichia coli:dnaB exterior surface residues regulate DNA helicase behavior to maintain genomic stability and organismal fitness." PLOS Genetics 17, no. 11 (2021): e1009886. http://dx.doi.org/10.1371/journal.pgen.1009886.

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Helicase regulation involves modulation of unwinding speed to maintain coordination of DNA replication fork activities and is vital for replisome progression. Currently, mechanisms for helicase regulation that involve interactions with both DNA strands through a steric exclusion and wrapping (SEW) model and conformational shifts between dilated and constricted states have been examined in vitro. To better understand the mechanism and cellular impact of helicase regulation, we used CRISPR-Cas9 genome editing to study four previously identified SEW-deficient mutants of the bacterial replicative

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18

Lin, Hsin-Hsien, and Cheng-Yang Huang. "Characterization of Flavonol Inhibition of DnaB Helicase: Real-Time Monitoring, Structural Modeling, and Proposed Mechanism." Journal of Biomedicine and Biotechnology 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/735368.

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DnaB helicases are motor proteins essential for DNA replication, repair, and recombination and may be a promising target for developing new drugs for antibiotic-resistant bacteria. Previously, we established that flavonols significantly decreased the binding ability ofKlebsiella pneumoniaeDnaB helicase (KpDnaB) to dNTP. Here, we further investigated the effect of flavonols on the inhibition of the ssDNA binding, ATPase activity, and dsDNA-unwinding activity ofKpDnaB. The ssDNA-stimulated ATPase activity ofKpDnaB was decreased to 59%, 75%, 65%, and 57%, in the presence of myricetin, quercetin,

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19

Arias-Palomo, Ernesto, Valerie L. O’Shea, Iris V. Hood, and James M. Berger. "The Bacterial DnaC Helicase Loader Is a DnaB Ring Breaker." Cell 153, no. 2 (2013): 438–48. http://dx.doi.org/10.1016/j.cell.2013.03.006.

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20

Hanada, Katsuhiro, Teruhito Yamashita, Yuko Shobuike, and Hideo Ikeda. "Role of DnaB Helicase in UV-Induced Illegitimate Recombination in Escherichia coli." Journal of Bacteriology 183, no. 17 (2001): 4964–69. http://dx.doi.org/10.1128/jb.183.17.4964-4969.2001.

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ABSTRACT To study the involvement of DNA replication in UV-induced illegitimate recombination, we examined the effect of temperature-sensitive dnaB mutations on illegitimate recombination and found that the frequency of illegitimate recombination was reduced by an elongation-deficient mutation,dnaB14, but not by an initiation-deficient mutation,dnaB252. This result indicates that DNA replication is required for UV-induced illegitimate recombination. In addition, thednaB14 mutation also affected spontaneous or UV-induced illegitimate recombination enhanced by the recQmutation. Nucleotide sequen

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21

Shadrick, William R., Jean Ndjomou, Rajesh Kolli, Sourav Mukherjee, Alicia M. Hanson, and David N. Frick. "Discovering New Medicines Targeting Helicases." Journal of Biomolecular Screening 18, no. 7 (2013): 761–81. http://dx.doi.org/10.1177/1087057113482586.

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Helicases are ubiquitous motor proteins that separate and/or rearrange nucleic acid duplexes in reactions fueled by adenosine triphosphate (ATP) hydrolysis. Helicases encoded by bacteria, viruses, and human cells are widely studied targets for new antiviral, antibiotic, and anticancer drugs. This review summarizes the biochemistry of frequently targeted helicases. These proteins include viral enzymes from herpes simplex virus, papillomaviruses, polyomaviruses, coronaviruses, the hepatitis C virus, and various flaviviruses. Bacterial targets examined include DnaB-like and RecBCD-like helicases.

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22

Miller, Christine, and Stanley N. Cohen. "Separate Roles of Escherichia coliReplication Proteins in Synthesis and Partitioning of pSC101 Plasmid DNA." Journal of Bacteriology 181, no. 24 (1999): 7552–57. http://dx.doi.org/10.1128/jb.181.24.7552-7557.1999.

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ABSTRACT We report here that the Escherichia coli replication proteins DnaA, which is required to initiate replication of both the chromosome and plasmid pSC101, and DnaB, the helicase that unwinds strands during DNA replication, have effects on plasmid partitioning that are distinct from their functions in promoting plasmid DNA replication. Temperature-sensitive dnaB mutants cultured under conditions permissive for DNA replication failed to partition plasmids normally, and when cultured under conditions that prevent replication, they showed loss of the entire multicopy pool of plasmid replico

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23

Yamashita, Teruhito, Katsuhiro Hanada, Mihoko Iwasaki, Hirotaka Yamaguchi, and Hideo Ikeda. "Illegitimate Recombination Induced by Overproduction of DnaB Helicase in Escherichia coli." Journal of Bacteriology 181, no. 15 (1999): 4549–53. http://dx.doi.org/10.1128/jb.181.15.4549-4553.1999.

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ABSTRACT Illegitimate recombination that usually takes place at a low frequency is greatly enhanced by treatment with DNA-damaging agents. It is thought that DNA double-strand breaks induced by this DNA damage are important for initiation of illegitimate recombination. Here we show that illegitimate recombination is enhanced by overexpression of the DnaB protein in Escherichia coli. The recombination enhanced by DnaB overexpression occurred between short regions of homology. We propose a model for the initiation of illegitimate recombination in which DnaB overexpression may excessively unwind

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24

Slavcev, Roderick A., and Barbara E. Funnell. "Identification and Characterization of a Novel Allele of Escherichia coli dnaB Helicase That Compromises the Stability of Plasmid P1." Journal of Bacteriology 187, no. 4 (2005): 1227–37. http://dx.doi.org/10.1128/jb.187.4.1227-1237.2005.

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ABSTRACT Bacteriophage P1 lysogenizes Escherichia coli cells as a plasmid with approximately the same copy number as the copy number of the host chromosome. Faithful inheritance of the plasmids relies upon proper DNA replication, as well as a partition system that actively segregates plasmids to new daughter cells. We genetically screened for E. coli chromosomal mutations that influenced P1 stability and identified a novel temperature-sensitive allele of the dnaB helicase gene (dnaB277) that replaces serine 277 with a leucine residue (DnaB S277L). This allele conferred a severe temperature-sen

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25

Soni, R. K. "Functional characterization of Helicobacter pylori DnaB helicase." Nucleic Acids Research 31, no. 23 (2003): 6828–40. http://dx.doi.org/10.1093/nar/gkg895.

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26

Biswas, Esther E., Marjorie H. Barnes, Donald T. Moir, and Subhasis B. Biswas. "An Essential DnaB Helicase of Bacillus anthracis: Identification, Characterization, and Mechanism of Action." Journal of Bacteriology 191, no. 1 (2008): 249–60. http://dx.doi.org/10.1128/jb.01259-08.

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ABSTRACT We have described a novel essential replicative DNA helicase from Bacillus anthracis, the identification of its gene, and the elucidation of its enzymatic characteristics. Anthrax DnaB helicase (DnaBBA) is a 453-amino-acid, 50-kDa polypeptide with ATPase and DNA helicase activities. DnaBBA displayed distinct enzymatic and kinetic properties. DnaBBA has low single-stranded DNA (ssDNA)-dependent ATPase activity but possesses a strong 5′→3′ DNA helicase activity. The stimulation of ATPase activity appeared to be a function of the length of the ssDNA template rather than of ssDNA binding

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27

Sandler, Steven J. "Multiple Genetic Pathways for Restarting DNA Replication Forks in Escherichia coli K-12." Genetics 155, no. 2 (2000): 487–97. http://dx.doi.org/10.1093/genetics/155.2.487.

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Abstract In Escherichia coli, the primosome assembly proteins, PriA, PriB, PriC, DnaT, DnaC, DnaB, and DnaG, are thought to help to restart DNA replication forks at recombinational intermediates. Redundant functions between priB and priC and synthetic lethality between priA2::kan and rep3 mutations raise the possibility that there may be multiple pathways for restarting replication forks in vivo. Herein, it is shown that priA2::kan causes synthetic lethality when placed in combination with either Δrep::kan or priC303:kan. These determinations were made using a nonselective P1 transduction-base

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28

Donate, Luis-Enrique, Óscar Llorca, Montserrat Bárcena, Susan E. Brown, Nicholas E. Dixon, and José-Marı́a Carazo. "pH-controlled quaternary states of hexameric DnaB helicase." Journal of Molecular Biology 303, no. 3 (2000): 383–93. http://dx.doi.org/10.1006/jmbi.2000.4132.

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29

Carr, Kevin M., and Jon M. Kaguni. "Escherichia coliDnaA Protein Loads a Single DnaB Helicase at a DnaA Box Hairpin." Journal of Biological Chemistry 277, no. 42 (2002): 39815–22. http://dx.doi.org/10.1074/jbc.m205031200.

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30

Delagoutte, Emmanuelle, and Peter H. von Hippel. "Helicase mechanisms and the coupling of helicases within macromolecular machines Part II: Integration of helicases into cellular processes." Quarterly Reviews of Biophysics 36, no. 1 (2003): 1–69. http://dx.doi.org/10.1017/s0033583502003864.

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Анотація:

1. Helicases as components of macromolecular machines 32. Helicases in replication 72.1 The loading of replicative helicases 72.1.1 Loading Rep helicase at the replication origin of bacteriophage ϕX174 72.1.2 How is a ssDNA strand passed through (and bound in?) the central channel of the hexameric replicative helicases? 82.1.3 Loading of E. coli DnaB helicase in the absence of an auxiliary protein-loading factor 82.1.4 The T7 gp4 primase-helicase is loaded by means of a facilitated ring-opening mechanism 102.1.5 Bacteriophage T4 gp61 primase can be viewed as a loading factor for the homologous

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31

Zhang, Yi, Fude Yang, Yeh-Chih Kao, Michael G. Kurilla, David L. Pompliano, and Ira B. Dicker. "Homogenous Assays for Escherichia coli DnaB-Stimulated DnaG Primase and DnaB Helicase and Their Use in Screening for Chemical Inhibitors." Analytical Biochemistry 304, no. 2 (2002): 174–79. http://dx.doi.org/10.1006/abio.2002.5627.

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32

Sandler, Steven J., Hardeep S. Samra, and Alvin J. Clark. "Differential Suppression of priA2::kan Phenotypes in Escherichia coli K-12 by Mutations in priA, lexA, and dnaC." Genetics 143, no. 1 (1996): 5–13. http://dx.doi.org/10.1093/genetics/143.1.5.

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Abstract First identified as an essential component of the ϕX174 in vitro DNA replication system, PriA has ATPase, helicase, translocase, and primosome-assembly activities. priA1::kan strains of Escherichia coli are sensitive to UV irradiation, deficient in homologous recombination following transduction, and filamentous. priA2::kan strains have eightfold higher levels of uninduced SOS expression than wild type. We show that (1) priA1::kan strains have eightfold higher levels of uninduced SOS expression, (2) priA2::kan strains are UVS and Rec−, (3) lexA3 suppresses the high basal levels of SOS

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33

Weigel, Christoph, and Harald Seitz. "Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC." Molecular Microbiology 46, no. 4 (2002): 1149–56. http://dx.doi.org/10.1046/j.1365-2958.2002.03232.x.

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Bailey, S., W. K. Eliason, and T. A. Steitz. "Structure of Hexameric DnaB Helicase and Its Complex with a Domain of DnaG Primase." Science 318, no. 5849 (2007): 459–63. http://dx.doi.org/10.1126/science.1147353.

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35

Poggi, Silvana, and Sathees Chandra. "Genomics Analysis of Replicative Helicase DnaB Sequences in Proteobacteria." Acta Informatica Medica 22, no. 4 (2014): 249. http://dx.doi.org/10.5455/aim.2014.22.249-254.

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36

Bujalowski, Wlodzimierz. "Expanding the physiological role of the hexameric DnaB helicase." Trends in Biochemical Sciences 28, no. 3 (2003): 116–18. http://dx.doi.org/10.1016/s0968-0004(03)00034-3.

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37

Santamarı́a, David, Guillermo de la Cueva, Marı́a Luisa Martı́nez-Robles, Dora B. Krimer, Pablo Hernández, and Jorge B. Schvartzman. "DnaB Helicase Is Unable to Dissociate RNA-DNA Hybrids." Journal of Biological Chemistry 273, no. 50 (1998): 33386–96. http://dx.doi.org/10.1074/jbc.273.50.33386.

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38

Griep, Mark A., Sheldon Blood, Marilynn A. Larson, Scott A. Koepsell, and Steven H. Hinrichs. "Myricetin inhibits Escherichia coli DnaB helicase but not primase." Bioorganic & Medicinal Chemistry 15, no. 22 (2007): 7203–8. http://dx.doi.org/10.1016/j.bmc.2007.07.057.

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39

Belle, Jerilyn J., Andrew Casey, Charmain T. Courcelle, and Justin Courcelle. "Inactivation of the DnaB Helicase Leads to the Collapse and Degradation of the Replication Fork: a Comparison to UV-Induced Arrest." Journal of Bacteriology 189, no. 15 (2007): 5452–62. http://dx.doi.org/10.1128/jb.00408-07.

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ABSTRACT Replication forks face a variety of structurally diverse impediments that can prevent them from completing their task. The mechanism by which cells overcome these hurdles is likely to vary depending on the nature of the obstacle and the strand in which the impediment is encountered. Both UV-induced DNA damage and thermosensitive replication proteins have been used in model systems to inhibit DNA replication and characterize the mechanism by which it recovers. In this study, we examined the molecular events that occur at replication forks following inactivation of a thermosensitive Dna

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40

Neylon, Cameron, Andrew V. Kralicek, Thomas M. Hill, and Nicholas E. Dixon. "Replication Termination in Escherichia coli: Structure and Antihelicase Activity of the Tus-Ter Complex." Microbiology and Molecular Biology Reviews 69, no. 3 (2005): 501–26. http://dx.doi.org/10.1128/mmbr.69.3.501-526.2005.

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SUMMARY The arrest of DNA replication in Escherichia coli is triggered by the encounter of a replisome with a Tus protein-Ter DNA complex. A replication fork can pass through a Tus-Ter complex when traveling in one direction but not the other, and the chromosomal Ter sites are oriented so replication forks can enter, but not exit, the terminus region. The Tus-Ter complex acts by blocking the action of the replicative DnaB helicase, but details of the mechanism are uncertain. One proposed mechanism involves a specific interaction between Tus-Ter and the helicase that prevents further DNA unwind

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41

Bailey, Scott, William K. Eliason, and Thomas A. Steitz. "The crystal structure of the Thermus aquaticus DnaB helicase monomer." Nucleic Acids Research 35, no. 14 (2007): 4728–36. http://dx.doi.org/10.1093/nar/gkm507.

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42

Bujalowski, W., M. M. Klonowska, and M. J. Jezewska. "Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein." Journal of Biological Chemistry 269, no. 50 (1994): 31350–58. http://dx.doi.org/10.1016/s0021-9258(18)31701-0.

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43

Johnson, Scott K., Saumitri Bhattacharyya, and Mark A. Griep. "DnaB Helicase Stimulates Primer Synthesis Activity on Short Oligonucleotide Templates†." Biochemistry 39, no. 4 (2000): 736–44. http://dx.doi.org/10.1021/bi991554l.

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44

Ribeck, Noah, Daniel L. Kaplan, Irina Bruck, and Omar A. Saleh. "DnaB Helicase Activity Is Modulated by DNA Geometry and Force." Biophysical Journal 99, no. 7 (2010): 2170–79. http://dx.doi.org/10.1016/j.bpj.2010.07.039.

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45

LeBowitz, J. H., and R. McMacken. "The Escherichia coli dnaB replication protein is a DNA helicase." Journal of Biological Chemistry 261, no. 10 (1986): 4738–48. http://dx.doi.org/10.1016/s0021-9258(17)38564-2.

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46

Itsathitphaisarn, Ornchuma, Richard A. Wing, William K. Eliason, Jimin Wang, and Thomas A. Steitz. "The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation." Cell 151, no. 2 (2012): 267–77. http://dx.doi.org/10.1016/j.cell.2012.09.014.

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47

Chen, Cheng-Chieh, and Cheng-Yang Huang. "Inhibition of Klebsiella Pneumoniae DnaB Helicase by the Flavonol Galangin." Protein Journal 30, no. 1 (2011): 59–65. http://dx.doi.org/10.1007/s10930-010-9302-0.

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48

Marsin, Stéphanie, Yazid Adam, Claire Cargemel, et al. "Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase." Nucleic Acids Research 49, no. 11 (2021): 6569–86. http://dx.doi.org/10.1093/nar/gkab463.

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Abstract Replicative helicases are essential proteins that unwind DNA in front of replication forks. Their loading depends on accessory proteins and in bacteria, DnaC and DnaI are well characterized loaders. However, most bacteria do not express either of these two proteins. Instead, they are proposed to rely on DciA, an ancestral protein unrelated to DnaC/I. While the DciA structure from Vibrio cholerae shares no homology with DnaC, it reveals similarities with DnaA and DnaX, two proteins involved during replication initiation. As other bacterial replicative helicases, VcDnaB adopts a toroid-

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49

Bianco, Piero R. "DNA Helicase-SSB Interactions Critical to the Regression and Restart of Stalled DNA Replication Forks in Escherichia coli." Genes 11, no. 5 (2020): 471. http://dx.doi.org/10.3390/genes11050471.

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In Escherichia coli, DNA replication forks stall on average once per cell cycle. When this occurs, replisome components disengage from the DNA, exposing an intact, or nearly intact fork. Consequently, the fork structure must be regressed away from the initial impediment so that repair can occur. Regression is catalyzed by the powerful, monomeric DNA helicase, RecG. During this reaction, the enzyme couples unwinding of fork arms to rewinding of duplex DNA resulting in the formation of a Holliday junction. RecG works against large opposing forces enabling it to clear the fork of bound proteins.

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50

Sakamoto, Y., S. Nakai, S. Moriya, H. Yoshikawa, and N. Ogasawara. "The Bacillus subtilis dnaC gene encodes a protein homologous to the DnaB helicase of Escherichia coli." Microbiology 141, no. 3 (1995): 641–44. http://dx.doi.org/10.1099/13500872-141-3-641.

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