Auxiliary ATP binding sites support DNA unwinding by RecBCD (original) (raw)

Auxiliary ATP binding sites power rapid unwinding by RecBCD

Ariel Kaplan

View PDFchevron_right

RecBCD possesses strong coupling between DNA and nucleotide binding that may propel a stepping mechanism during translocation

Or Dvir

View PDFchevron_right

Influence of DNA End Structure on the Mechanism of Initiation of DNA Unwinding by the Escherichia coli RecBCD and RecBC Helicases

Timothy Lohman

Journal of Molecular Biology, 2008

View PDFchevron_right

Synergy between RecBCD subunits is essential for efficient DNA unwinding

Ariel Kaplan

eLife, 2019

View PDFchevron_right

The RecD Subunit of the RecBCD Enzyme from Escherichia coli Is a Single-stranded DNA-dependent ATPase

Biao Ruan

Journal of Biological Chemistry, 1997

View PDFchevron_right

ATPase Cycle and DNA Unwinding Kinetics of RecG Helicase

Martin R Webb

PLoS ONE, 2012

View PDFchevron_right

Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding

Timothy Lohman

2004

View PDFchevron_right

DNA unwinding heterogeneity by RecBCD results from static molecules able to equilibrate

Bian Liu

Nature

View PDFchevron_right

Interactions of RadB, a DNA Repair Protein in Archaea, with DNA and ATP

Sam Haldenby

Journal of Molecular Biology, 2006

View PDFchevron_right

Quantitative genomic analysis of RecA protein binding during DNA double-strand break repair reveals RecBCD action in vivo

Milana Filatenkova

2015

View PDFchevron_right

The ATPase activity of E. coli RecA prevents accumulation of toxic complexes formed by erroneous binding to undamaged double stranded DNA

Jeffrey Carey

Nucleic Acids Research

View PDFchevron_right

Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli

Firouzeh Korangy

Journal of Biological Chemistry, 1992

View PDFchevron_right

Alteration by site-directed mutagenesis of the conserved lysine residue in the consensus ATP-binding sequence of the RecB protein ofEscherichia coli

Firouzeh Korangy

Nucleic Acids Research, 1992

View PDFchevron_right

Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor

Timothy Lohman

Nature structural & molecular biology, 2010

View PDFchevron_right

Energetics of DNA End Binding by E. coli RecBC and RecBCD Helicases Indicate Loop Formation in the 30-Single-stranded DNA Tail

Timothy Lohman

J Mol Biol, 2005

View PDFchevron_right

Energetics of DNA End Binding by E.coli RecBC and RecBCD Helicases Indicate Loop Formation in the 3′-Single-stranded DNA Tail

Timothy Lohman

Journal of Molecular Biology, 2005

View PDFchevron_right

RecBCD and RecJ/RecQ Initiate DNA Degradation on Distinct Substrates in UV-Irradiated Escherichia coli

Kin-Hoe Chow

Radiation Research, 2007

View PDFchevron_right

ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex

Aera Jo

The EMBO journal, 2015

View PDFchevron_right

Evidence for ATP binding and double-stranded DNA binding by Escherichia coli RecF protein

Alvin Clark

Journal of Bacteriology, 1992

View PDFchevron_right

E. coliRecBCD Nuclease Domain Regulates Helicase Activity but not Single Stranded DNA Translocase Activity

Timothy Lohman

bioRxiv (Cold Spring Harbor Laboratory), 2023

View PDFchevron_right

Unwinding and rewinding of DNA by the RecBC enzyme

Alison Taylor

Cell, 1980

View PDFchevron_right

MAW point mutation impairs H. Seropedicae RecA ATP hydrolysis and DNA repair without inducing large conformational changes in its structure

Sérgio Saab

PLOS ONE

View PDFchevron_right

Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli

S. Lovett

Genes & Development, 2009

View PDFchevron_right

ATPase Activity of Escherichia coli Rep Helicase Is Dramatically Dependent on DNA Ligation and Protein Oligomeric States †

Isaac Wong

Biochemistry, 1996

View PDFchevron_right

ATP half-sites in RadA and RAD51 recombinases bind nucleotides

Tom Blundell

FEBS open bio, 2016

View PDFchevron_right

A two-site kinetic mechanism for ATP binding and hydrolysis by E. coli rep helicase dimer bound to a single-stranded oligodeoxynucleotide

Timothy Lohman

Journal of Molecular Biology, 1999

View PDFchevron_right

RecO and RecR are necessary for RecA loading in response to DNA damage and replication fork stress

Roderick Sorenson

Journal of bacteriology, 2014

View PDFchevron_right

Reversible Induction of ATP Synthesis by DNA Damage and Repair in Escherichia coli

Hadassa Degani

Journal of Biological Chemistry, 1998

View PDFchevron_right

Asymmetric Regulation of Bipolar Single-stranded DNA Translocation by the Two Motors within Escherichia coli RecBCD Helicase

Timothy Lohman

Journal of Biological Chemistry, 2013

View PDFchevron_right

Reversible Induction of ATP Synthesis by DNA Damage and Repair in Escherichia coli. IN VIVO NMR STUDIES

Zehava Eichenbaum

Journal of Biological Chemistry, 1998

View PDFchevron_right

Single molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB

debjani bagchi

View PDFchevron_right

ATPase Mechanism of the 5′-3′ DNA Helicase, RecD2

Martin R Webb

Journal of Biological Chemistry, 2013

View PDFchevron_right

Mutual Inhibition of RecQ Molecules in DNA Unwinding

Bing Yi Pan

Journal of Biological Chemistry, 2010

View PDFchevron_right

Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding

Ingar Leiros, Joanna Timmins

The EMBO Journal, 2007

View PDFchevron_right