2005
DOI: 10.1016/j.mrfmmm.2005.03.013
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‘Close-fitting sleeves’: DNA damage recognition by the UvrABC nuclease system

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Cited by 126 publications
(134 citation statements)
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“…The above analysis may be further elaborated in the context of recent structural data obtained for B. subtilis UvrB*, which shows domain 1-3 in contact with a domain 4 dimer. In that structure (PDB code 2D7D) the long axis of domain 4 is roughly parallel to the long axis of UvrB [1][2][3] , and is apparently positioned by two salt bridges. This interface between domains 3 and 4 is quite insubstantial, however, such a tenuous interface would be consistent with the crystal structures in which domain 4 is generally not observed.…”
Section: Discussionmentioning
confidence: 99%
“…The above analysis may be further elaborated in the context of recent structural data obtained for B. subtilis UvrB*, which shows domain 1-3 in contact with a domain 4 dimer. In that structure (PDB code 2D7D) the long axis of domain 4 is roughly parallel to the long axis of UvrB [1][2][3] , and is apparently positioned by two salt bridges. This interface between domains 3 and 4 is quite insubstantial, however, such a tenuous interface would be consistent with the crystal structures in which domain 4 is generally not observed.…”
Section: Discussionmentioning
confidence: 99%
“…Damage recognition in the nucleotide excision repair pathway is an ATP-dependent multi-step process, for recent reviews see [1][2][3]. While several models have been proposed for prokaryotic damage recognition, most suggest that UvrA, as part of an UvrA 2 B or UvrA 2 B 2 complex [4], first scans DNA for altered base-pair conformations.…”
Section: Introductionmentioning
confidence: 99%
“…Based on these findings, it is conceivable that a ternary complex involving XPC, XPA, and TFIIH scans DNA strands to search for damage: this model is reminiscent of the damage-recognition mechanism in the bacterial NER system. As for E. coli, 2 damage recognition pathways have been proposed (Van Houten et al, 2005): the UvrA homodimer directly recognizes and binds to distorted sites and then recruits UvrB, or preassembled complexes involving 2 UvrA and 1 or 2 UvrB molecules bind DNA in a nonspecific manner and then search for damage by scanning the DNA strands. In this analogy, UvrB seems to correspond to TFIIH as the driving subunit with ATPase/helicase activities, whereas UvrA may have evolved into XPC and/or XPA.…”
Section: Roles For Tfiih Helicases In Damage Verificationmentioning
confidence: 99%