The fifth essential DNA polymerase phi in Saccharomyces cerevisiae is localized to the nucleolus and plays an important role in synthesis of rRNA

K Shimizu, Y Kawasaki, SI Hiraga, M Tawaramoto, N Nakashima, A Sugino

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Abstract

We report that POL5 encodes the fifth essential DNA polymerase in Saccharomyces cerevisiae. Pol5p was identified and purified from yeast cell extracts and is an aphidicolin-sensitive DNA polymerase that is stimulated by yeast proliferating cell nuclear antigen (PCNA). Thus, we named Pol5p DNA polymerase φ. Temperature-sensitive pol5-1∼–3 mutants did not arrest at G2/M at the restrictive temperature. Furthermore, the polymerase active-site mutant POL5dn gene complements the lethality of Δpol5. These results suggest that the polymerase activity of Pol5p is not required for the in vivo function of Pol5p. rRNA synthesis was severely inhibited at the restrictive temperature in the temperature-sensitive pol5-3 mutant cells, suggesting that an essential function of Pol5p is rRNA synthesis. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.
Original languageEnglish
Pages (from-to)9133-9138
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number14
DOIs
Publication statusPublished - 9 Jul 2002

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DNA-Directed DNA Polymerase
Saccharomyces cerevisiae
Temperature
Yeasts
Aphidicolin
Proliferating Cell Nuclear Antigen
Cell Extracts
Catalytic Domain
DNA
Genes

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The fifth essential DNA polymerase phi in Saccharomyces cerevisiae is localized to the nucleolus and plays an important role in synthesis of rRNA. / Shimizu, K; Kawasaki, Y; Hiraga, SI; Tawaramoto, M; Nakashima, N; Sugino, A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, No. 14, 09.07.2002, p. 9133-9138.

Research output: Contribution to journalArticle

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abstract = "We report that POL5 encodes the fifth essential DNA polymerase in Saccharomyces cerevisiae. Pol5p was identified and purified from yeast cell extracts and is an aphidicolin-sensitive DNA polymerase that is stimulated by yeast proliferating cell nuclear antigen (PCNA). Thus, we named Pol5p DNA polymerase φ. Temperature-sensitive pol5-1∼–3 mutants did not arrest at G2/M at the restrictive temperature. Furthermore, the polymerase active-site mutant POL5dn gene complements the lethality of Δpol5. These results suggest that the polymerase activity of Pol5p is not required for the in vivo function of Pol5p. rRNA synthesis was severely inhibited at the restrictive temperature in the temperature-sensitive pol5-3 mutant cells, suggesting that an essential function of Pol5p is rRNA synthesis. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.",
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