The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity.
about
Structural mechanisms of PriA-mediated DNA replication restartIdentification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein.Multiple C-terminal tails within a single E. coli SSB homotetramer coordinate DNA replication and repair.A Replisome's journey through the bacterial chromosome.Bacillus subtilis RecA and its accessory factors, RecF, RecO, RecR and RecX, are required for spore resistance to DNA double-strand break.Mechanisms of bacterial DNA replication restart.Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicaseBacillus subtilis RarA modulates replication restart
P2860
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P2860
The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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2012年论文
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name
The PriA replication restart p ...... y through its ATPase activity.
@ast
The PriA replication restart p ...... y through its ATPase activity.
@en
type
label
The PriA replication restart p ...... y through its ATPase activity.
@ast
The PriA replication restart p ...... y through its ATPase activity.
@en
prefLabel
The PriA replication restart p ...... y through its ATPase activity.
@ast
The PriA replication restart p ...... y through its ATPase activity.
@en
P2860
P356
P1476
The PriA replication restart p ...... y through its ATPase activity.
@en
P2093
Carol M Manhart
Charles S McHenry
P2860
P304
P356
10.1074/JBC.M112.435966
P407
P577
2012-12-20T00:00:00Z