Literature DB >> 16532007

Structural basis for DNA recognition and processing by UvrB.

James J Truglio1, Erkan Karakas, Benjamin Rhau, Hong Wang, Matthew J DellaVecchia, Bennett Van Houten, Caroline Kisker.   

Abstract

DNA-damage recognition in the nucleotide excision repair (NER) cascade is a complex process, operating on a wide variety of damages. UvrB is the central component in prokaryotic NER, directly involved in DNA-damage recognition and guiding the DNA through repair synthesis. We report the first structure of a UvrB-double-stranded DNA complex, providing insights into the mechanism by which UvrB binds DNA, leading to formation of the preincision complex. One DNA strand, containing a 3' overhang, threads behind a beta-hairpin motif of UvrB, indicating that this motif inserts between the strands of the double helix, thereby locking down either the damaged or undamaged strand. The nucleotide directly behind the beta-hairpin is flipped out and inserted into a small, highly conserved pocket in UvrB.

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Year:  2006        PMID: 16532007     DOI: 10.1038/nsmb1072

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN: 1545-9985            Impact factor:   15.369


  54 in total

1.  Structure and mechanism of the UvrA-UvrB DNA damage sensor.

Authors:  Danaya Pakotiprapha; Martin Samuels; Koning Shen; Johnny H Hu; David Jeruzalmi
Journal:  Nat Struct Mol Biol       Date:  2012-02-05       Impact factor: 15.369

2.  Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.

Authors:  Erkan Karakas; James J Truglio; Deborah Croteau; Benjamin Rhau; Liqun Wang; Bennett Van Houten; Caroline Kisker
Journal:  EMBO J       Date:  2007-01-24       Impact factor: 11.598

3.  Base flipping free energy profiles for damaged and undamaged DNA.

Authors:  Han Zheng; Yuqin Cai; Shuang Ding; Yijin Tang; Konstantin Kropachev; Yanzi Zhou; Lihua Wang; Shenglong Wang; Nicholas E Geacintov; Yingkai Zhang; Suse Broyde
Journal:  Chem Res Toxicol       Date:  2010-12-20       Impact factor: 3.739

4.  Preprotein-controlled catalysis in the helicase motor of SecA.

Authors:  Spyridoula Karamanou; Giorgos Gouridis; Efrosyni Papanikou; Giorgos Sianidis; Ioannis Gelis; Dimitra Keramisanou; Eleftheria Vrontou; Charalampos G Kalodimos; Anastassios Economou
Journal:  EMBO J       Date:  2007-05-24       Impact factor: 11.598

Review 5.  On helicases and other motor proteins.

Authors:  Eric J Enemark; Leemor Joshua-Tor
Journal:  Curr Opin Struct Biol       Date:  2008-03-10       Impact factor: 6.809

6.  Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding.

Authors:  Danaya Pakotiprapha; Yoshihiko Inuzuka; Brian R Bowman; Geri F Moolenaar; Nora Goosen; David Jeruzalmi; Gregory L Verdine
Journal:  Mol Cell       Date:  2007-12-27       Impact factor: 17.970

7.  Stimulation of UvrD helicase by UvrAB.

Authors:  John Atkinson; Colin P Guy; Chris J Cadman; Geri F Moolenaar; Nora Goosen; Peter McGlynn
Journal:  J Biol Chem       Date:  2009-02-10       Impact factor: 5.157

8.  A structural model for the damage-sensing complex in bacterial nucleotide excision repair.

Authors:  Danaya Pakotiprapha; Yi Liu; Gregory L Verdine; David Jeruzalmi
Journal:  J Biol Chem       Date:  2009-03-13       Impact factor: 5.157

Review 9.  Prokaryotic nucleotide excision repair.

Authors:  Caroline Kisker; Jochen Kuper; Bennett Van Houten
Journal:  Cold Spring Harb Perspect Biol       Date:  2013-03-01       Impact factor: 10.005

10.  NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution.

Authors:  Matthew J DellaVecchia; W Keither Merritt; Ye Peng; Thomas W Kirby; Eugene F DeRose; Geoffrey A Mueller; Bennett Van Houten; Robert E London
Journal:  J Mol Biol       Date:  2007-08-02       Impact factor: 5.469

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