A novel heterotetrameric structure of the crenarchaeal PCNA2–PCNA3 complex

Kawai, Akito; Hashimoto, Hiroshi; Higuchi, Shigesada; Tsunoda, Masaru; Sato, Mamoru; Nakamura, Kazuo; Miyamoto, Shuichi

doi:10.1016/j.jsb.2011.02.006

Cited by 13 publications

(16 citation statements)

References 48 publications

(58 reference statements)

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“…The superposition shows that large parts of the structures accurately match and that the complexes share the size and shape of the central channel as well as the twist observed between the heterodimeric planes of the archaeal structure. It has been hypothesized that the central channel of the archaeal complex can accommodate two stacked DNA duplexes and thus may clamp a Holliday junction (Kawai et al., 2011). To the viral processivity factor, a multifunctional role in virus replication has been ascribed (Sugimoto et al., 2011; Kawashima et al., 2013).…”

Section: Resultsmentioning

confidence: 99%

“…(D) 1czd@1 (homotrimer; Moarefi et al., 2000), a DNA polymerase accessory protein from Enterobacteria phage T4. (E) 3aiz@1 (heterotetramer; Kawai et al., 2011), a DNA polymerase sliding clamp from Sulfolobus tokodaii . (F) 2z0l@8 (homotetramer; Murayama et al., 2009), a DNA polymerase processivity factor from human herpesvirus 4.…”

Section: Figurementioning

confidence: 99%

“…(Left) 3aiz@1 (Kawai et al., 2011), a heterotetrameric DNA polymerase sliding clamp from S. tokodaii .…”

Section: Figurementioning

confidence: 99%

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Structure-Based Characterization of Multiprotein Complexes

et al. 2014

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SummaryMultiprotein complexes govern virtually all cellular processes. Their 3D structures provide important clues to their biological roles, especially through structural correlations among protein molecules and complexes. The detection of such correlations generally requires comprehensive searches in databases of known protein structures by means of appropriate structure-matching techniques. Here, we present a high-speed structure search engine capable of instantly matching large protein oligomers against the complete and up-to-date database of biologically functional assemblies of protein molecules. We use this tool to reveal unseen structural correlations on the level of protein quaternary structure and demonstrate its general usefulness for efficiently exploring complex structural relationships among known protein assemblies.

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Section: Resultsmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Structure-Based Characterization of Multiprotein Complexes

et al. 2014

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“…Crenarcheal homologs, such as that from Sulfolobus solfataricus , are heterotrimers composed of subunits PCNA1, PCNA2, and PCNA3 [59, 60] (Figure 1(d)). A recent study suggested the possibility that PCNA from Sulfolobus tokodaii forms a heterotetramer from two PCNA2-PCNA3 complexes [61]. …”

Section: Dna Replication and Repairmentioning

confidence: 99%

Archaeal Genome Guardians Give Insights into Eukaryotic DNA Replication and Damage Response Proteins

Shin

Pratt

Tainer

2014

Archaea

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As the third domain of life, archaea, like the eukarya and bacteria, must have robust DNA replication and repair complexes to ensure genome fidelity. Archaea moreover display a breadth of unique habitats and characteristics, and structural biologists increasingly appreciate these features. As archaea include extremophiles that can withstand diverse environmental stresses, they provide fundamental systems for understanding enzymes and pathways critical to genome integrity and stress responses. Such archaeal extremophiles provide critical data on the periodic table for life as well as on the biochemical, geochemical, and physical limitations to adaptive strategies allowing organisms to thrive under environmental stress relevant to determining the boundaries for life as we know it. Specifically, archaeal enzyme structures have informed the architecture and mechanisms of key DNA repair proteins and complexes. With added abilities to temperature-trap flexible complexes and reveal core domains of transient and dynamic complexes, these structures provide insights into mechanisms of maintaining genome integrity despite extreme environmental stress. The DNA damage response protein structures noted in this review therefore inform the basis for genome integrity in the face of environmental stress, with implications for all domains of life as well as for biomanufacturing, astrobiology, and medicine.

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“…In contrast, heterotrimeric PCNAs have been characterised in crenarchaea, with each subunit binding specific partners [5]. Recent work suggests variation in formation of the protein rings that can occur in crenarchaea [6]. This variety is a crucial resource in understanding the mode of action of PCNA and other sliding clamps.…”

Section: The Structure Of Pcna Is Globally Conserved Between the Amentioning

confidence: 99%

Rings in the Extreme: PCNA Interactions and Adaptations in the Archaea

Winter

Bunting

2012

Archaea

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Biochemical and structural analysis of archaeal proteins has enabled us to gain great insight into many eukaryotic processes, simultaneously offering fascinating glimpses into the adaptation and evolution of proteins at the extremes of life. The archaeal PCNAs, central to DNA replication and repair, are no exception. Characterisation of the proteins alone, and in complex with both peptides and protein binding partners, has demonstrated the diversity and subtlety in the regulatory role of these sliding clamps. Equally, studies have provided valuable detailed insight into the adaptation of protein interactions and mechanisms that are necessary for life in extreme environments.

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A novel heterotetrameric structure of the crenarchaeal PCNA2–PCNA3 complex

Cited by 13 publications

References 48 publications

Structure-Based Characterization of Multiprotein Complexes

Structure-Based Characterization of Multiprotein Complexes

Archaeal Genome Guardians Give Insights into Eukaryotic DNA Replication and Damage Response Proteins

Rings in the Extreme: PCNA Interactions and Adaptations in the Archaea

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