In Vivo Analysis of Functional Regions within Yeast Rap1p

Graham, Ian R.; Haw, R; Spink, Karen G.; Halden, Kathryn A.; Chambers, A.

doi:10.1128/mcb.19.11.7481

Cited by 49 publications

(74 citation statements)

References 67 publications

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“…This strain was supplemented with a single copy plasmid encompassing variants of the Rap1p protein expressed from its natural promoter. In this background, the episomal Rap1p variant is the only Rap1p source when the cells are grown in glucose (25). The results for three of these variants, as well as for an intact copy of the RAP1 gene, are shown in Fig.…”

Section: Dissection Of the C-terminal Domain Of Rap1p-strainmentioning

confidence: 89%

“…Sequences of all constructs were determined by the T7 polymerase method (Amersham Pharmacia Biotech). Plasmids pRAP, pRAP⌬Sil, and pRAP⌬Tox have been described elsewhere (25).…”

Section: Plasmids and Strainsmentioning

confidence: 99%

“…This domain is the target for interactions with telomeric proteins Rif1p, Rif2p, Sir2p, Sir3p, and Sir4p (26, 28 -31). Finally, deletion of amino acids 597-629 (the Tox domain) has minor physiological effects but increases the amount of mutated Rap1p present in the cell (25,26). It also eliminates the cellular toxicity produced by the overexpression of Rap1p both in Saccharomyces cerevisiae and in Schizosaccharomyces pombe (32,33).…”

mentioning

confidence: 99%

“…3 for a review). Analysis in vivo of the functional regions within Rap1p revealed that the DNA-binding domain (amino acids 342-596) is the only portion of Rap1p essential for growth (25). However, removal of the so-called activation (Act) domain (amino acids 627-690, (26)) strongly decreases growth rates and compromises the transcription of several, but not all, Rap1p-regulated genes (25).…”

mentioning

confidence: 99%

“…However, removal of the so-called activation (Act) domain (amino acids 627-690, (26)) strongly decreases growth rates and compromises the transcription of several, but not all, Rap1p-regulated genes (25). Deletion of the so-called silencing (Sil) domain (amino acids 700 -798) results in a milder growth defect, an increase in the transcription of several Rap1p-regulated genes, and the loss of transcriptional silencing through Rap1p both at telomeres and at the HML and HMR loci (25)(26)(27). This domain is the target for interactions with telomeric proteins Rif1p, Rif2p, Sir2p, Sir3p, and Sir4p (26, 28 -31).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Alternative Mechanisms of Transcriptional Activation by Rap1p

Idrissi

García-Reyero

Fernández-Larrea

et al. 2001

Journal of Biological Chemistry

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Section: Dissection Of the C-terminal Domain Of Rap1p-strainmentioning

confidence: 89%

“…Sequences of all constructs were determined by the T7 polymerase method (Amersham Pharmacia Biotech). Plasmids pRAP, pRAP⌬Sil, and pRAP⌬Tox have been described elsewhere (25).…”

Section: Plasmids and Strainsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Alternative Mechanisms of Transcriptional Activation by Rap1p

Idrissi

García-Reyero

Fernández-Larrea

et al. 2001

Journal of Biological Chemistry

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Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment

Orbea

Syme

et al. 2005

Proteomics

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In an attempt to improve the detection of peroxisome proliferation as a biomarker in environmental pollution assessment, we have applied a novel approach based on peroxisomal proteomics. Peroxisomal proteins from digestive glands of mussels Mytilus galloprovincialis were analyzed using 2-DE and MS. We have generated a reference 2-DE map from samples obtained in a well-studied reference area and compared this with peroxisomal proteomes from other sequenced genomes. In addition, by comparing 2-DE maps from control samples with samples obtained in a polluted area, we have characterized the peroxisome proliferation expression pattern associated with exposure to a polluted environment. Over 100 spots were reproducibly resolved per 2-DE map; 55 differentially expressed spots were quantitatively detected and analyzed, and 14 of these showed an increase in protein expression of more than fourfold. Epoxide hydrolase, peroxisomal antioxidant enzyme, and sarcosine oxidase (SOX) have been identified by ESI MS/MS, and acyl-CoA oxidase, multifunctional protein, and Cu,Zn-superoxide dismutase were immunolocalized by Western blotting. Our results indicate that a peroxisomal protein pattern associated to marine pollutant exposure can be generated, and this approach may have a greater potential as biomarker than traditional, single-protein markers.

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Isolation and characterization of Candida albicans homologue of RAP1, a repressor and activator protein gene in Saccharomyces cerevisiae.

Uemura

Watanabe-Yoshida²,

Ishii³

et al. 2003

Yeast

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To study the function of RAP1, a Candida albicans gene (CaRAP1 ) that shows sequence similarity to RAP1 of Saccharomyces cerevisiae was isolated by colony hybridization. DNA sequencing predicted an open reading frame of 429 amino acids with an overall identity of 24% to the ScRap1p. The DNA binding domain (DBD) was highly conserved, and EMSA using a GST-CaRap1p fusion protein confirmed its binding ability to the RPG-box of S. cerevisiae ENO1. In contrast, the N-terminus was less conserved and a moderate homology was observed in the BRCT domain. Interestingly, CaRap1p did not contain the C-terminal activation/repression region of ScRap1p. Its DDBJ/EMBL/GenBank Accession No. is AB036055.

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In Vivo Analysis of Functional Regions within Yeast Rap1p

Cited by 49 publications

References 67 publications

Alternative Mechanisms of Transcriptional Activation by Rap1p

Alternative Mechanisms of Transcriptional Activation by Rap1p

Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment

Isolation and characterization of Candida albicans homologue of RAP1, a repressor and activator protein gene in Saccharomyces cerevisiae.

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