PCNA Loading by RFC, Mechanism of

Muse Oke; Manal Zaher; Samir Hamdan

doi:10.1007/978-1-4614-1531-2_137

PCNA Loading by RFC, Mechanism of

Muse Oke, Manal Zaher, Samir Hamdan

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Replicative polymerases achieve highly processive DNA synthesis by binding to a clamp-like processivity factor that is topologically linked to DNA. The eukaryotic processivity clamp, proliferating cell nuclear antigen (PCNA), exists mostly as a closed ring in solution. Replication factor C (RFC), a five-subunit ATP-dependent protein complex, mediates PCNA opening in solution (assembly stage) and closing onto the primer-template (disassembly stage). In the assembly stage, RFC binding to ATP causes conformational changes that trigger RFC to form a complex with PCNA. PCNA is then cracked open at one subunit interface, and both RFC and PCNA adopt an extended spiral structure with a chamber that selects for a primer-template DNA structure. Binding of RFC/PCNA to DNA triggers the disassembly stage by stimulating ATP hydrolysis. Subsequent conformational changes in RFC and PCNA lead to the closing of PCNA onto the primer-template and the dissociation of RFC.

Original language	English (US)
Title of host publication	Molecular Life Sciences
Publisher	Springer Nature
Pages	861-866
Number of pages	6
ISBN (Print)	9781461415299
DOIs	https://doi.org/10.1007/978-1-4614-1531-2_137
State	Published - Jan 30 2018

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KAUST Repository Item: Exported on 2020-10-01

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10.1007/978-1-4614-1531-2_137

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abstract = "Replicative polymerases achieve highly processive DNA synthesis by binding to a clamp-like processivity factor that is topologically linked to DNA. The eukaryotic processivity clamp, proliferating cell nuclear antigen (PCNA), exists mostly as a closed ring in solution. Replication factor C (RFC), a five-subunit ATP-dependent protein complex, mediates PCNA opening in solution (assembly stage) and closing onto the primer-template (disassembly stage). In the assembly stage, RFC binding to ATP causes conformational changes that trigger RFC to form a complex with PCNA. PCNA is then cracked open at one subunit interface, and both RFC and PCNA adopt an extended spiral structure with a chamber that selects for a primer-template DNA structure. Binding of RFC/PCNA to DNA triggers the disassembly stage by stimulating ATP hydrolysis. Subsequent conformational changes in RFC and PCNA lead to the closing of PCNA onto the primer-template and the dissociation of RFC.",

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AU - Hamdan, Samir

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N2 - Replicative polymerases achieve highly processive DNA synthesis by binding to a clamp-like processivity factor that is topologically linked to DNA. The eukaryotic processivity clamp, proliferating cell nuclear antigen (PCNA), exists mostly as a closed ring in solution. Replication factor C (RFC), a five-subunit ATP-dependent protein complex, mediates PCNA opening in solution (assembly stage) and closing onto the primer-template (disassembly stage). In the assembly stage, RFC binding to ATP causes conformational changes that trigger RFC to form a complex with PCNA. PCNA is then cracked open at one subunit interface, and both RFC and PCNA adopt an extended spiral structure with a chamber that selects for a primer-template DNA structure. Binding of RFC/PCNA to DNA triggers the disassembly stage by stimulating ATP hydrolysis. Subsequent conformational changes in RFC and PCNA lead to the closing of PCNA onto the primer-template and the dissociation of RFC.

AB - Replicative polymerases achieve highly processive DNA synthesis by binding to a clamp-like processivity factor that is topologically linked to DNA. The eukaryotic processivity clamp, proliferating cell nuclear antigen (PCNA), exists mostly as a closed ring in solution. Replication factor C (RFC), a five-subunit ATP-dependent protein complex, mediates PCNA opening in solution (assembly stage) and closing onto the primer-template (disassembly stage). In the assembly stage, RFC binding to ATP causes conformational changes that trigger RFC to form a complex with PCNA. PCNA is then cracked open at one subunit interface, and both RFC and PCNA adopt an extended spiral structure with a chamber that selects for a primer-template DNA structure. Binding of RFC/PCNA to DNA triggers the disassembly stage by stimulating ATP hydrolysis. Subsequent conformational changes in RFC and PCNA lead to the closing of PCNA onto the primer-template and the dissociation of RFC.

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ER -

PCNA Loading by RFC, Mechanism of

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