Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus

Felice, Maurilio De; Sensen, Christoph Wilhelm; Charlebois, Robert L.; Rossi, Mosè; Pisani, Francesca M.

doi:10.1006/jmbi.1999.2939

Cited by 50 publications

(44 citation statements)

References 44 publications

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“…Sso PCNA 039 and Sso PCNA 048 (20). We carried out polymerase activity assays using an oligo(dT)-primed poly(dA) template (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The length of synthesized tracks was more than 200 nucleotides at the highest concentration of pol Y1. Because Sso PCNA 039p and 048p possess trimeric structures and conserve several functionally important motifs with eukaryotic counterparts (20), the results may have implications in the eukaryotic members of Y-type DNA polymerases. In fact, Haracska et al (44) reported that interaction with PCNA is essential for yeast DNA polymerase function.…”

Section: Discussionmentioning

confidence: 99%

“…The use of a sliding clamp to increase the processivity of DNA polymerases is a common strategy in Archaea, prokaryotes, and eukaryotes (20,42,43). The clamps tether DNA polymerase molecules to a template/primer DNA, thereby preventing the falling off of polymerases from template DNA.…”

Section: Discussionmentioning

confidence: 99%

“…The Sso RFC complex, Sso PCNA 039, and Sso PCNA 048 proteins were purified as described previously (20,25). Reactions were carried out for 10 min at 60°C and terminated by adding stop solution as in the primer extension assay.…”

Section: Methodsmentioning

confidence: 99%

“…As evidenced by the genome sequencing project, many eukaryotic replication proteins have close homologues in Archaea (18,19). Interestingly, the thermoacidophilic archaebacterium Sulfolobus solfataricus possesses two PCNA-like sliding clamps termed Sso 039p (244 amino acids, 27 kDa) and Sso 048p (249 amino acids, 27 kDa) (20). Both proteins possess a trimeric structure, which is similar to eukaryotic PCNAs, and functions as a processivity factor that stimulates the activity of monomeric family B DNA polymerases from this organism (Sso DNA polymerase B1) (21)(22)(23)(24) by enhancing processivity.…”

mentioning

confidence: 99%

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Synthetic Activity of Sso DNA Polymerase Y1, an Archaeal DinB-like DNA Polymerase, Is Stimulated by Processivity Factors Proliferating Cell Nuclear Antigen and Replication Factor C

Grúz¹,

Pisani²,

Shimizu³

et al. 2001

Journal of Biological Chemistry

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DNA replication efficiency is dictated by DNA polymerases (pol) and their associated proteins. The recent discovery of DNA polymerase Y family (DinB/UmuC/ RAD30/REV1 superfamily) raises a question of whether the DNA polymerase activities are modified by accessory proteins such as proliferating cell nuclear antigen (PCNA). In fact, the activity of DNA pol IV (DinB) of Escherichia coli is enhanced upon interaction with the ␤ subunit, the processivity factor of DNA pol III. Here, we report the activity of Sso DNA pol Y1 encoded by the dbh gene of the archaeon Sulfolobus solfataricus is greatly enhanced by the presence of PCNA and replication factor C (RFC). Sso pol Y1 per se was a distributive enzyme but a substantial increase in the processivity was observed on poly(dA)-oligo(dT) in the presence of PCNA (039p or 048p) and RFC. The length of the synthesized DNA product reached at least 200 nucleotides. Sso pol Y1 displayed a higher affinity for DNA compared with pol IV of E. coli, suggesting that the two DNA polymerases have distinct reason(s) to require the processivity factors for efficient DNA synthesis. The abilities of pol Y1 and pol IV to bypass DNA lesions and their sensitive sites to protease are also discussed.The recently identified novel family of DNA polymerases (pol) 1 (DinB/UmuC/Rev1/Rad30 superfamily or family Y) comprises proteins from different species including Bacteria, Eukarya, and Archaea (1, 2). Members of this superfamily can bypass lesions on template DNA, such as ultraviolet light photoproducts, and mismatched primer/template DNA (3-7). Thus, the new DNA polymerases seem to function by assisting the conventional DNA replicases to cope with faulty DNA templates by taking over the DNA synthesis at aberrant sites (for recent reviews, see Refs. 1 and 8 -12). Common features of family Y DNA polymerases include the lack of 3Ј-exonuclease proofreading activity and synthesis of DNA with low fidelity in a distributive fashion. The human DNA pol has been shown recently to possess 5Ј-deoxyribose phosphate lyase activity, suggesting a role in base excision repair (13). It has been hypothesized that the very low processivity of these polymerases prevents excessive introduction of mutations because of extended error-prone DNA synthesis. This has been, however, questioned recently when DNA polymerase IV of Escherichia coli (pol IV) (7) was found to synthesize tracks of more than 300 nucleotides upon interaction with the ␤ subunit of pol III (14). The ␤ subunit and its eukaryotic counterpart, i.e. PCNA, play essential roles in processive chromosomal replication by forming a sliding platform that mediates the interaction of DNA polymerases with DNA (15). In addition, the sliding clamps also interact with a variety of proteins other than DNA polymerases involved in DNA processing and even in cell cycle control (16). It is therefore of general interest to elucidate the relationships between various members of Y family DNA polymerases and the corresponding sliding clamps.Archaea, the third domain of life, is t...

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“…Sso PCNA 039 and Sso PCNA 048 (20). We carried out polymerase activity assays using an oligo(dT)-primed poly(dA) template (Fig.…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Synthetic Activity of Sso DNA Polymerase Y1, an Archaeal DinB-like DNA Polymerase, Is Stimulated by Processivity Factors Proliferating Cell Nuclear Antigen and Replication Factor C

Grúz¹,

Pisani²,

Shimizu³

et al. 2001

Journal of Biological Chemistry

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The PCNA from Thermococcus fumicolans Functionally Interacts with DNA Polymerase δ

Henneke

Raffin

Ferrari

et al. 2000

Biochemical and Biophysical Research Communications

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We have cloned the gene encoding proliferating cell nuclear antigen (PCNA) from the hyperthermophilic euryarchaeote Thermococcus fumicolans (Tfu). Tfu PCNA contains 250 amino acids with a calculated M(r) of 28,000 and is 26% identical to human PCNA. Next, Tfu PCNA was overexpressed in Escherichia coli and it showed an apparent molecular mass of 33.5 kDa. The purified Tfu PCNA was tested first with recombinant Tfu DNA polymerase I (Tfu pol) and second with calf thymus DNA polymerase delta (pol delta). When tested with the homologous Tfu pol on bacteriophage lambda DNA, large amounts of Tfu PCNA were required to obtain two- to threefold stimulation. Surprisingly, however, Tfu PCNA was much more efficient than human PCNA in stimulating calf thymus pol delta. Our data suggest that PCNA has been functionally conserved not only within eukaryotes but also from hyperthermophilic euryarchaeotes to mammals.

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Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus 1 1Edited by M. Gottesman

Pisani

Felice

Carpentieri

et al. 2000

Journal of Molecular Biology

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Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus

Cited by 50 publications

References 44 publications

Synthetic Activity of Sso DNA Polymerase Y1, an Archaeal DinB-like DNA Polymerase, Is Stimulated by Processivity Factors Proliferating Cell Nuclear Antigen and Replication Factor C

Synthetic Activity of Sso DNA Polymerase Y1, an Archaeal DinB-like DNA Polymerase, Is Stimulated by Processivity Factors Proliferating Cell Nuclear Antigen and Replication Factor C

The PCNA from Thermococcus fumicolans Functionally Interacts with DNA Polymerase δ

Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus 1 1Edited by M. Gottesman

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