Rep provides a second motor at the replisome to promote duplication of protein-bound DNA.
Mol Cell
; 36(4): 654-66, 2009 Nov 25.
Article
en En
| MEDLINE
| ID: mdl-19941825
ABSTRACT
Nucleoprotein complexes present challenges to genome stability by acting as potent blocks to replication. One attractive model of how such conflicts are resolved is direct targeting of blocked forks by helicases with the ability to displace the blocking protein-DNA complex. We show that Rep and UvrD each promote movement of E. coli replisomes blocked by nucleoprotein complexes in vitro, that such an activity is required to clear protein blocks (primarily transcription complexes) in vivo, and that a polarity of translocation opposite that of the replicative helicase is critical for this activity. However, these two helicases are not equivalent. Rep but not UvrD interacts physically and functionally with the replicative helicase. In contrast, UvrD likely provides a general means of protein-DNA complex turnover during replication, repair, and recombination. Rep and UvrD therefore provide two contrasting solutions as to how organisms may promote replication of protein-bound DNA.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
ADN Bacteriano
/
ADN Helicasas
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Proteínas Motoras Moleculares
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Proteínas de Escherichia coli
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ADN Polimerasa Dirigida por ADN
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Complejos Multienzimáticos
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2009
Tipo del documento:
Article
País de afiliación:
Reino Unido