Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis

Tomoko Miyata, Hirofumi Suzuki, Takuji Oyama, Kouta Mayanagi, Yoshizumi Ishino, Kosuke Morikawa

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

Ring-shaped sliding clamps and clamp loader ATPases are essential factors for rapid and accurate DNA replication. The clamp ring is opened and reseated at the primer-template junctions by the ATP-fueled clamp loader function. The processivity of the DNA polymerase is conferred by its attachment to the clamp loaded onto the DNA. In eukarya and archaea, the replication factor C (RFC) and the proliferating cell nuclear antigen (PCNA) play crucial roles as the clamp loader and the clamp, respectively. Here, we report the electron microscopic structure of an archaeal RFC-PCNA-DNA complex at 12-Å resolution. This complex exhibits excellent fitting of each atomic structure of RFC, PCNA, and the primed DNA. The PCNA ring retains an open conformation by extensive interactions with RFC, with a distorted spring washer-like conformation. The complex appears to represent the intermediate, where the PCNA ring is kept open before ATP hydrolysis by RFC.

Original languageEnglish
Pages (from-to)13795-13800
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number39
DOIs
Publication statusPublished - Sep 27 2005

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Replication Protein C
Proliferating Cell Nuclear Antigen
Electrons
DNA
Adenosine Triphosphate
Archaea
DNA-Directed DNA Polymerase
Eukaryota
DNA Replication
Adenosine Triphosphatases
Hydrolysis

All Science Journal Classification (ASJC) codes

  • General

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Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. / Miyata, Tomoko; Suzuki, Hirofumi; Oyama, Takuji; Mayanagi, Kouta; Ishino, Yoshizumi; Morikawa, Kosuke.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, No. 39, 27.09.2005, p. 13795-13800.

Research output: Contribution to journalArticle

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