Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5′- to 3′-exonuclease required for lagging strand DNA synthesis in reconstituted systems

Christopher H. Sommers, Edward J. Miller, Bernard Dujon, Satya Prakash, Louise Prakash

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162 Citations (Scopus)

Abstract

A 5′- to 3′-exonuclease of about 45 kDa has been purified from various mammalian sources and shown to be required for the completion of lagging strand synthesis in reconstituted DNA replication systems. RTH1 encodes the yeast Saccharomyces cerevisiae counterpart of the mammalian enzyme. To determine the in vivo biological role of RTH1-encoded 5′- to 3′-exonuclease, we have examined the effects of an rth1Δ mutation on various cellular processes. rth1Δ mutants grow poorly at 30°C, and a cessation in growth occurs upon transfer of the mutant to 37°C. At the restrictive temperature, the rth1Δ mutant exhibits a terminal cell cycle morphology similar to that of mutants defective in DNA replication, and levels of spontaneous mitotic recombination are elevated in the rth1Δ mutant even at the permissive temperature. The rth1Δ mutation does not affect UV or γ-ray sensitivity but enhances sensitivity to the alkylating agent methyl methanesulfonate. The role of RTH1 in DNA replication and in repair of alkylation damage is discussed.

Original languageEnglish (US)
Pages (from-to)4193-4196
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number9
StatePublished - Mar 3 1995

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spleen exonuclease
Exonucleases
DNA Replication
Yeast
Yeasts
Mutation
DNA
Methyl Methanesulfonate
Temperature
Alkylating Agents
Alkylation
Genetic Recombination
Saccharomyces cerevisiae
Cell Cycle
Repair
Cells
Enzymes
Growth

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5′- to 3′-exonuclease required for lagging strand DNA synthesis in reconstituted systems",
abstract = "A 5′- to 3′-exonuclease of about 45 kDa has been purified from various mammalian sources and shown to be required for the completion of lagging strand synthesis in reconstituted DNA replication systems. RTH1 encodes the yeast Saccharomyces cerevisiae counterpart of the mammalian enzyme. To determine the in vivo biological role of RTH1-encoded 5′- to 3′-exonuclease, we have examined the effects of an rth1Δ mutation on various cellular processes. rth1Δ mutants grow poorly at 30°C, and a cessation in growth occurs upon transfer of the mutant to 37°C. At the restrictive temperature, the rth1Δ mutant exhibits a terminal cell cycle morphology similar to that of mutants defective in DNA replication, and levels of spontaneous mitotic recombination are elevated in the rth1Δ mutant even at the permissive temperature. The rth1Δ mutation does not affect UV or γ-ray sensitivity but enhances sensitivity to the alkylating agent methyl methanesulfonate. The role of RTH1 in DNA replication and in repair of alkylation damage is discussed.",
author = "Sommers, {Christopher H.} and Miller, {Edward J.} and Bernard Dujon and Satya Prakash and Louise Prakash",
year = "1995",
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T1 - Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5′- to 3′-exonuclease required for lagging strand DNA synthesis in reconstituted systems

AU - Sommers, Christopher H.

AU - Miller, Edward J.

AU - Dujon, Bernard

AU - Prakash, Satya

AU - Prakash, Louise

PY - 1995/3/3

Y1 - 1995/3/3

N2 - A 5′- to 3′-exonuclease of about 45 kDa has been purified from various mammalian sources and shown to be required for the completion of lagging strand synthesis in reconstituted DNA replication systems. RTH1 encodes the yeast Saccharomyces cerevisiae counterpart of the mammalian enzyme. To determine the in vivo biological role of RTH1-encoded 5′- to 3′-exonuclease, we have examined the effects of an rth1Δ mutation on various cellular processes. rth1Δ mutants grow poorly at 30°C, and a cessation in growth occurs upon transfer of the mutant to 37°C. At the restrictive temperature, the rth1Δ mutant exhibits a terminal cell cycle morphology similar to that of mutants defective in DNA replication, and levels of spontaneous mitotic recombination are elevated in the rth1Δ mutant even at the permissive temperature. The rth1Δ mutation does not affect UV or γ-ray sensitivity but enhances sensitivity to the alkylating agent methyl methanesulfonate. The role of RTH1 in DNA replication and in repair of alkylation damage is discussed.

AB - A 5′- to 3′-exonuclease of about 45 kDa has been purified from various mammalian sources and shown to be required for the completion of lagging strand synthesis in reconstituted DNA replication systems. RTH1 encodes the yeast Saccharomyces cerevisiae counterpart of the mammalian enzyme. To determine the in vivo biological role of RTH1-encoded 5′- to 3′-exonuclease, we have examined the effects of an rth1Δ mutation on various cellular processes. rth1Δ mutants grow poorly at 30°C, and a cessation in growth occurs upon transfer of the mutant to 37°C. At the restrictive temperature, the rth1Δ mutant exhibits a terminal cell cycle morphology similar to that of mutants defective in DNA replication, and levels of spontaneous mitotic recombination are elevated in the rth1Δ mutant even at the permissive temperature. The rth1Δ mutation does not affect UV or γ-ray sensitivity but enhances sensitivity to the alkylating agent methyl methanesulfonate. The role of RTH1 in DNA replication and in repair of alkylation damage is discussed.

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