Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition

EMBO Journal

Volumn 20, Issue 3, 2001, Pages 601-611

  Verhoeven, Esther E A ^a   Wyman, Claire ^b   Moolenaar, Geri F ^a   Hoeijmakers, Jan H J ^b   Goosen, Nora ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b ERASMUS MEDICAL CENTER   (Netherlands)

Author keywords

Atomic force microscopy; Damage recognition; Escherichia coli; Nucleotide excision repair; UvrABC

Indexed keywords

ARTICLE; ATOMIC FORCE MICROSCOPY; COMPLEX FORMATION; DNA DAMAGE; ESCHERICHIA COLI; EXCISION REPAIR; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; ULTRAVIOLET A RADIATION; ULTRAVIOLET B RADIATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BASE SEQUENCE; DNA HELICASES; DNA PRIMERS; DNA REPAIR; DNA, BACTERIAL; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA;

ESCHERICHIA COLI;

EID: 0035254673     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.3.601     Document Type: Article

References (29)

1. Topological unwinding of strong and weak promoters by RNA polymerase. A comparison between the lac wild-type and the UV5 sites of Escherichia coli
2. Identification of the different intermediates in the interaction of (A)BC excinuclease with its substrates by DNase I footprinting on two uniquely modified oligonucleotides
3. Structural basis for initiation of transcription from an RNA polymerase-promoter complex
4. DNA bending and wrapping around RNA polymerase: A 'revolutionary' model describing transcriptional mechanisms
5. Transcriptional activation by E.coli CAP protein
6. The Fis protein: It's not just for DNA inversion anymore
7. The regulation of transcription initiation by integration host factor
8. Functional domains of the Escherichia coli UvrABC proteins in nucleotide excision repair
9. Active site of (A)BC excinuclease. I. Evidence for 5′ incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues
10. Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
11. Dimerization of Escherichia coli UvrA and its binding to undamaged and ultraviolet light damaged DNA
12. Characterization of the Escherichia coli damage-independent UvrBC endonuclease activity
13. The effect of the DNA flanking the lesion on formation of the UvrB-DNA preincision complex. Mechanism for the UvrA-mediated loading of UvrB onto the damage
14. The role of ATP binding and hydrolysis by UvrB during nucleotide excision repair
15. Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair
16. Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I
17. Wrapping of DNA around the E.coli RNA polymerase open promoter complex
18. DNA excision repair
19. Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex
20. Structure of UvrABC excinuclease-UV-damaged DNA complexes studied by flow linear dichroism. DNA curved by UvrB and UvrC
21. Crystal structure of UvrB, a helicase adapted for nucleotide excision repair
22. Evidence for DNA bending at the T7 RNA polymerase promoter
23. Nucleotide excision repair in Escherichia coli
24. DNase I footprint of ABC excinuclease
25. Catalytic sites for 3′ and 5′ incision of Escherichia coli nucleotide excision repair are both located in UvrC
26. Uvr excision repair protein complex of Escherichia coli binds to the convex side of a cisplatin-induced kink in the DNA
27. Analysis of UvrABC endonuclease reaction intermediates on cisplatin-damaged DNA using mobility shift gel electrophoresis
28. 2B complex allows dynamic recognition of DNA damage
29. Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-(+)- or dG-(-)-anti-BPDE