Literature DB >> 8994032

Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase.

J A Ali1, T M Lohman.   

Abstract

The kinetic mechanism by which the DNA repair helicase UvrD of Escherichia coli unwinds duplex DNA was examined with the use of a series of oligodeoxynucleotides with duplex regions ranging from 10 to 40 base pairs. Single-turnover unwinding experiments showed distinct lag phases that increased with duplex length because partially unwound DNA intermediate states are highly populated during unwinding. Analysis of these kinetics indicates that UvrD unwinds duplex DNA in discrete steps, with an average "step size" of 4 to 5 base pairs (approximately one-half turn of the DNA helix). This suggests an unwinding mechanism in which alternating subunits of the dimeric helicase interact directly with duplex DNA.

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Year:  1997        PMID： 8994032     DOI： 10.1126/science.275.5298.377

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  116 in total

1.  Visualization of unwinding activity of duplex RNA by DbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy.

Authors:  Arnon Henn; Ohad Medalia; Shu-Ping Shi; Michal Steinberg; Francois Franceschi; Irit Sagi
Journal:  Proc Natl Acad Sci U S A       Date:  2001-04-10       Impact factor: 11.205

2.  Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement.

Authors:  K Firman; M D Szczelkun
Journal:  EMBO J       Date:  2000-05-02       Impact factor: 11.598

3.  Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.

Authors:  G Sianidis; S Karamanou; E Vrontou; K Boulias; K Repanas; N Kyrpides; A S Politou; A Economou
Journal:  EMBO J       Date:  2001-03-01       Impact factor: 11.598

Review 4.  Modularity and specialization in superfamily 1 and 2 helicases.

Authors:  Martin R Singleton; Dale B Wigley
Journal:  J Bacteriol       Date:  2002-04       Impact factor: 3.490

5.  Rearrangement of structured RNA via branch migration structures catalysed by the highly related DEAD-box proteins p68 and p72.

Authors:  O G Rössler; A Straka; H Stahl
Journal:  Nucleic Acids Res       Date:  2001-05-15       Impact factor: 16.971

6.  Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor.

Authors:  Bindu Nanduri; Alicia K Byrd; Robert L Eoff; Alan J Tackett; Kevin D Raney
Journal:  Proc Natl Acad Sci U S A       Date:  2002-10-31       Impact factor: 11.205

Review 7.  Single-molecule views of protein movement on single-stranded DNA.

Authors:  Taekjip Ha; Alexander G Kozlov; Timothy M Lohman
Journal:  Annu Rev Biophys       Date:  2012-02-23       Impact factor: 12.981

8.  Measurement of steady-state kinetic parameters for DNA unwinding by the bacteriophage T4 Dda helicase: use of peptide nucleic acids to trap single-stranded DNA products of helicase reactions.

Authors:  B Nanduri; R L Eoff; A J Tackett; K D Raney
Journal:  Nucleic Acids Res       Date:  2001-07-01       Impact factor: 16.971

9.  Guidelines for the selection of highly effective siRNA sequences for mammalian and chick RNA interference.

Authors:  Kumiko Ui-Tei; Yuki Naito; Fumitaka Takahashi; Takeshi Haraguchi; Hiroko Ohki-Hamazaki; Aya Juni; Ryu Ueda; Kaoru Saigo
Journal:  Nucleic Acids Res       Date:  2004-02-09       Impact factor: 16.971

10.  The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently.

Authors:  David N Frick; Ryan S Rypma; Angela M I Lam; Baohua Gu
Journal:  J Biol Chem       Date:  2003-10-29       Impact factor: 5.157
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