DOI: 10.1016/j.jmb.2003.12.031. DNA-binding Orientation and Domain Conformation of the E.coli Rep Helicase Monomer Bound to a Partial Duplex Junction: Single-molecule Studies of Fluorescently Labeled Enzymes

DNA-binding Orientation and Domain Conformation of the E.coli Rep Helicase Monomer Bound to a Partial Duplex Junction: Single-molecule Studies of Fluorescently Labeled Enzymes

10.1016/j.jmb.2003.12.031

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Rasnik, I., Myong, S., Cheng, W., Lohman, T. M., & Ha, T. (2004). DNA-binding Orientation and Domain Conformation of the E.coli Rep Helicase Monomer Bound to a Partial Duplex Junction: Single-molecule Studies of Fluorescently Labeled Enzymes. Journal of Molecular Biology, 336(2), 395â408.

Authors 5

Ivan Rasnik (first)
Sua Myong (additional)
Wei Cheng (additional)
Timothy M. Lohman (additional)
Taekjip Ha (additional)

References 27 Referenced 146

10.1006/jmbi.2001.4758 / J. Mol. Biol. / E.coli Rep oligomers are required to initiate DNA unwinding in vitro by Cheng (2001)
10.1038/nature01083 / Nature / Initiation and reinitiation of DNA unwinding by the Escherichia coli Rep helicase by Ha (2002)
10.1146/annurev.bi.65.070196.001125 / Annu. Rev. Biochem. / Mechanisms of helicase-catalyzed DNA unwinding by Lohman (1996)
10.1126/science.283.5408.1676 / Science / Fluorescence spectroscopy of single biomolecules by Weiss (1999)
10.1126/science.283.5408.1670 / Science / Illuminating single molecules in condensed matter by Moerner (1999)
10.1016/S0092-8674(00)80525-5 / Cell / Major domain swiveling revealed by the crystal structures of complexes of E.coli Rep helicase bound to single-stranded DNA and ATP by Korolev (1997)
10.1016/S0092-8674(00)80716-3 / Cell / Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism by Velankar (1999)
10.1038/384379a0 / Nature / Crystal structure of a Dexx box DNA helicase by Subramanya (1996)
10.1016/S0022-2836(02)01277-9 / J. Mol. Biol. / A dimer of Escherichia coli UvrD is the active form of the helicase in vitro by Maluf (2003)
10.1021/bi011137k / Biochemistry / Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine by Dillingham (2002)
10.1021/bi992105o / Biochemistry / Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed by Dillingham (2000)
10.1074/jbc.273.17.10515 / J. Biol. Chem. / Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli Dnab Helicase—fluorescence energy transfer studies by Jezewska (1998)
10.1073/pnas.74.1.193 / Proc. Natl Acad. Sci. USA / A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication by Scott (1977)
10.1006/meth.2001.1213 / Methods / Gel-based fluorescence resonance energy transfer (gelFRET) analysis of nucleoprotein complex architecture by Ramirez-Carrozzi (2001)
10.1021/ma971016l / Macromolecules / Poly(ethylen oxide) grafted to silicon surfaces: grafting density and protein adsorption by Sofia (1998)
10.1126/science.252.5009.1164 / Science / Self-assembled organic monolayers: model systems for studying adsorption of proteins at surfaces by Prime (1991)
10.1073/pnas.96.7.3670 / Proc. Natl Acad. Sci. USA / Single-pair fluorescence resonance energy transfer on freely diffusing molecules: observation of Forster distance dependence and subpopulations by Deniz (1999)
10.1073/pnas.96.3.893 / Proc. Natl Acad. Sci. USA / Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism by Ha (1999)
10.1016/S0092-8674(02)00667-0 / Cell / Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase–promoter open complex by Mekler (2002)
10.1038/nature01060 / Nature / Probing the free-energy surface for protein folding with single- molecule fluorescence spectroscopy by Schuler (2002)
10.1073/pnas.0434003100 / Proc. Natl Acad. Sci. USA / Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase:primer/template complexes by Rothwell (2003)
10.1016/0022-2836(91)90926-W / J. Mol. Biol. / DNA-induced dimerization of the Escherichia coli Rep helicase by Chao (1991)
10.1021/bi9719307 / Biochemistry / Kinetic mechanism for the sequential binding of two single-stranded oligodeoxynucleotides to the Escherichia coli Rep helicase dimer by Bjornson (1998)
10.1016/S0021-9258(19)40159-2 / J. Biol. Chem. / DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins by Chao (1990)
10.1073/pnas.242479399 / Proc. Natl Acad. Sci. USA / The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity by Cheng (2002)
10.1007/BF00329669 / Mol. Gen. Genet. / The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels by Colasant (1987)
10.1016/0076-6879(92)11020-J / Methods Enzymol. / Fluorescence resonance energy transfer and nucleic acids by Clegg (1992)

Dates

Type	When
Created	21 years, 8 months ago (Dec. 24, 2003, 5:36 a.m.)
Deposited	4 years, 2 months ago (June 13, 2021, 1:34 p.m.)
Indexed	1 year ago (Aug. 12, 2024, 8:31 a.m.)
Issued	21 years, 7 months ago (Feb. 1, 2004)
Published	21 years, 7 months ago (Feb. 1, 2004)
Published Print	21 years, 7 months ago (Feb. 1, 2004)

Funders 0

None

BibTeX

@article{Rasnik_2004, title={DNA-binding Orientation and Domain Conformation of the E.coli Rep Helicase Monomer Bound to a Partial Duplex Junction: Single-molecule Studies of Fluorescently Labeled Enzymes}, volume={336}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2003.12.031}, DOI={10.1016/j.jmb.2003.12.031}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Rasnik, Ivan and Myong, Sua and Cheng, Wei and Lohman, Timothy M. and Ha, Taekjip}, year={2004}, month=feb, pages={395–408} }

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