• Publications
  • Influence
Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicases
Background: The high speed and processivity of replicative DNA polymerases reside in a processivity factor which has been shown to be a ring‐shaped protein. This protein (‘sliding clamp’) encirclesExpand
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Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression
Single-molecule techniques are developed to examine mechanistic features of individual E. coli replisomes during synthesis of long DNA molecules. We find that single replisomes exhibit constant ratesExpand
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An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining.
Although three human genes encoding DNA ligases have been isolated, the molecular mechanisms by which these gene products specifically participate in different DNA transactions are not wellExpand
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Mechanism of polymerase collision release from sliding clamps on the lagging strand
Replicative polymerases are tethered to DNA by sliding clamps for processive DNA synthesis. Despite attachment to a sliding clamp, the polymerase on the lagging strand must cycle on and off DNA forExpand
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Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork
Eukaryotes use distinct polymerases for leading- and lagging-strand replication, but how they target their respective strands is uncertain. We reconstituted Saccharomyces cerevisiae replication forksExpand
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A Complex Consisting of Human Replication Factor C p40, p37, and p36 Subunits Is a DNA-dependent ATPase and an Intermediate in the Assembly of the Holoenzyme*
  • Jinsong Cai, E. Gibbs, +4 authors J. Hurwitz
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 25 July 1997
Human replication factor C (hRFC) is a multi-subunit protein complex capable of supporting proliferating cell nuclear antigen (PCNA)-dependent DNA synthesis by DNA polymerases δ and ε. The hRFCExpand
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Cost of rNTP/dNTP pool imbalance at the replication fork
The concentration of ribonucleoside triphosphates (rNTPs) in cells is far greater than the concentration of deoxyribonucleoside triphosphates (dNTPs), and this pool imbalance presents a challenge forExpand
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Mechanism of Proliferating Cell Nuclear Antigen Clamp Opening by Replication Factor C*
The eukaryotic replication factor C (RFC) clamp loader is an AAA+ spiral-shaped heteropentamer that opens and closes the circular proliferating cell nuclear antigen (PCNA) clamp processivity factorExpand
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Replication Factor C Clamp Loader Subunit Arrangement within the Circular Pentamer and Its Attachment Points to Proliferating Cell Nuclear Antigen*
Replication factor C (RFC) is a heteropentameric AAA+ protein clamp loader of the proliferating cell nuclear antigen (PCNA) processivity factor. The prokaryotic homologue, γ complex, is also aExpand
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The RFC clamp loader: structure and function.
The eukaryotic RFC clamp loader couples the energy of ATP hydrolysis to open and close the circular PCNA sliding clamp onto primed sites for use by DNA polymerases and repair factors. StructuralExpand
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