Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase

Eun Mi Kim, Yeun Kyu Jang, Sang Dai Park

Research output: Contribution to journalReview article

18 Citations (Scopus)

Abstract

Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that post-translational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.

Original languageEnglish
Pages (from-to)643-648
Number of pages6
JournalNucleic Acids Research
Volume30
Issue number3
Publication statusPublished - 2002 Feb 1

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Saccharomyces cerevisiae
Phosphotransferases
Phosphorylation
DNA Damage
Deoxyribodipyrimidine Photo-Lyase
Genes
Ribonucleotide Reductases
Zinc Fingers
Post Translational Protein Processing
Protein Kinases
Proteins

All Science Journal Classification (ASJC) codes

  • Genetics

Cite this

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title = "Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase",
abstract = "Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that post-translational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.",
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Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. / Kim, Eun Mi; Jang, Yeun Kyu; Park, Sang Dai.

In: Nucleic Acids Research, Vol. 30, No. 3, 01.02.2002, p. 643-648.

Research output: Contribution to journalReview article

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N2 - Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that post-translational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.

AB - Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that post-translational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.

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