Tomonori Takeuchi

Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae

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Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae. / Takeuchi, T; Miyahara, K; Hirata, D; Miyakawa, T.

In: FEBS Letters, Vol. 416, No. 3, 27.10.1997, p. 339-43.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Takeuchi, T, Miyahara, K, Hirata, D & Miyakawa, T 1997, 'Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae', FEBS Letters, vol. 416, no. 3, pp. 339-43.

APA

Takeuchi, T., Miyahara, K., Hirata, D., & Miyakawa, T. (1997). Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae. FEBS Letters, 416(3), 339-43.

CBE

MLA

Vancouver

Takeuchi T, Miyahara K, Hirata D, Miyakawa T. Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae. FEBS Letters. 1997 Oct 27;416(3):339-43.

Author

Takeuchi, T ; Miyahara, K ; Hirata, D ; Miyakawa, T. / Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae. In: FEBS Letters. 1997 ; Vol. 416, No. 3. pp. 339-43.

Bibtex

@article{95f2d059b2ae49fcafa01e067755aff9,
title = "Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae",
abstract = "To define the essential amino acid residues of Yap1 in stress response, we generated yap1 mutations by in vitro mutagenesis, which cause defects in mediating resistance to the stress of H2O2, but not of CdCl2. Sequence analysis of the mutant yap1 genes revealed three point mutations and two truncation mutations near the carboxy-terminus. The truncation mutations resulted in hyperresistance to cadmium. Northern blot analysis of stress-induced levels of TRX2 and GSH1 mRNAs indicated that the ability of the mutant Yap1 protein to induce transcriptional activation of target genes correlates well with its ability to confer stress resistance. The carboxy-terminal domain of Yap1 appears to act negatively in cadmium resistance.",
keywords = "Aminoacyltransferases/biosynthesis, Base Sequence, Binding Sites, Cadmium Chloride/pharmacology, DNA Mutational Analysis, DNA Primers, DNA-Binding Proteins/chemistry, Drug Resistance, Microbial, Fungal Proteins/chemistry, Hydrogen Peroxide/pharmacology, Hydroxylamine, Membrane Proteins/biosynthesis, Mutagenesis, Polymerase Chain Reaction, Saccharomyces cerevisiae/drug effects, Saccharomyces cerevisiae Proteins, Thioredoxins/biosynthesis, Transcription Factor AP-1/metabolism, Transcription Factors/chemistry, Transcription, Genetic, Transcriptional Activation",
author = "T Takeuchi and K Miyahara and D Hirata and T Miyakawa",
year = "1997",
month = "10",
day = "27",
language = "English",
volume = "416",
pages = "339--43",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Mutational analysis of Yap1 protein, an AP-1-like transcriptional activator of Saccharomyces cerevisiae

AU - Takeuchi, T

AU - Miyahara, K

AU - Hirata, D

AU - Miyakawa, T

PY - 1997/10/27

Y1 - 1997/10/27

N2 - To define the essential amino acid residues of Yap1 in stress response, we generated yap1 mutations by in vitro mutagenesis, which cause defects in mediating resistance to the stress of H2O2, but not of CdCl2. Sequence analysis of the mutant yap1 genes revealed three point mutations and two truncation mutations near the carboxy-terminus. The truncation mutations resulted in hyperresistance to cadmium. Northern blot analysis of stress-induced levels of TRX2 and GSH1 mRNAs indicated that the ability of the mutant Yap1 protein to induce transcriptional activation of target genes correlates well with its ability to confer stress resistance. The carboxy-terminal domain of Yap1 appears to act negatively in cadmium resistance.

AB - To define the essential amino acid residues of Yap1 in stress response, we generated yap1 mutations by in vitro mutagenesis, which cause defects in mediating resistance to the stress of H2O2, but not of CdCl2. Sequence analysis of the mutant yap1 genes revealed three point mutations and two truncation mutations near the carboxy-terminus. The truncation mutations resulted in hyperresistance to cadmium. Northern blot analysis of stress-induced levels of TRX2 and GSH1 mRNAs indicated that the ability of the mutant Yap1 protein to induce transcriptional activation of target genes correlates well with its ability to confer stress resistance. The carboxy-terminal domain of Yap1 appears to act negatively in cadmium resistance.

KW - Aminoacyltransferases/biosynthesis

KW - Base Sequence

KW - Binding Sites

KW - Cadmium Chloride/pharmacology

KW - DNA Mutational Analysis

KW - DNA Primers

KW - DNA-Binding Proteins/chemistry

KW - Drug Resistance, Microbial

KW - Fungal Proteins/chemistry

KW - Hydrogen Peroxide/pharmacology

KW - Hydroxylamine

KW - Membrane Proteins/biosynthesis

KW - Mutagenesis

KW - Polymerase Chain Reaction

KW - Saccharomyces cerevisiae/drug effects

KW - Saccharomyces cerevisiae Proteins

KW - Thioredoxins/biosynthesis

KW - Transcription Factor AP-1/metabolism

KW - Transcription Factors/chemistry

KW - Transcription, Genetic

KW - Transcriptional Activation

M3 - Journal article

C2 - 9373181

VL - 416

SP - 339

EP - 343

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 3

ER -