The 3'-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase

Journal of Molecular Biology

Volumn 301, Issue 2, 2000, Pages 285-299

  Kaplan, Daniel L ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

DNA replication fork; Helicase mechanism; Modified DNA; Nicked DNA; Unwinding assay

Indexed keywords

BACTERIAL DNA; HELICASE;

ARTICLE; CHEMICAL MODIFICATION; DNA DETERMINATION; DNA MODIFICATION; DNA REPLICATION; DNA STRAND; ENZYME ACTIVITY; ENZYME SYNTHESIS; MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN TRANSPORT; THERMUS AQUATICUS;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; THERMUS AQUATICUS;

EID: 0034636979     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3965     Document Type: Article

References (39)

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2. A general priming system employing only dnaB protein and primase for DNA replication
3. Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro
4. The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleotide triphosphate
5. Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
6. Crystal structure of the N-terminal domain of the DnaB hexameric helicase
7. Helicases: Amino acid sequence comparisons and structure-function relationships
8. A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
9. Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation
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11. Strand specificty in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork
12. Does single-stranded DNA pass through the inner channel of the protein hexamer in complex with the Escherichia coli DnaB helicase? Fluorescence energy transfer studies
13. Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: Recognition and structure
14. Duplex opening by primosome protein PriA for replisome assembly on a recombination intermediate
15. DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence
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17. The Escherichia coli dnaB replication protein is a DNA helicase
18. Escherichia coli replication termination protein impedes the action of helicases
19. PriA-directed assembly of a primosome on D Loop DNA
20. Replication fork assembly at recombination intermediates is required for bacterial growth
21. Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA
22. Helicase-contrahelicase interaction and the mechanism of termination of DNA replication
23. Three-dimensional reconstructions from cryoelectron microscopy images reveal and intimate complex between helicase DnaB and its loading partner DnaC
24. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
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27. The Escherichia coli pre-primosome and DNA B helicase can form replication forks that move at the same rate
28. DNA helicases displace streptavidin from biotin-labeled oligonucleotides
29. Characterization of the bacteriophage T4 gene 41 DNA helicase
30. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
31. The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA
32. The interaction between helicase and primase sets the replication fork clock
33. ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli
34. RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
35. Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase
36. NMR structure of the N-terminal domain of E. coli DnaB helicase: Implications for structure rearrangements in the helicase hexamer
37. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork: I. Multiple effectors act to modulate Okazaki fragment size
38. DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase
39. The hexameric E. coli DnaB helicase can exist in different quaternary states