Molecular characterization of the yeast meiotic regulatory gene<i>RIM1</i>

Su, Sophia Seh‐Yi; Mitchell, Aaron P.

doi:10.1093/nar/21.16.3789

Cited by 95 publications

(92 citation statements)

References 33 publications

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“…In this regard it might be noted that EFG1 lies downstream of TPK2, which encodes a cAMP-dependent protein kinase (35). Rim101p of S. cerevisiae contains a functionally significant recognition site for cAMP-dependent protein kinases (38). Although this site is not conserved in the C. albicans homolog, two potential phosphorylation sites are present, and this could provide a regulatory connection between TPK2, RIM101, and EFG1.…”

Section: Discussionmentioning

confidence: 99%

Dominant Active Alleles of RIM101(PRR2) Bypass the pH Restriction on Filamentation of Candida albicans

Barkani

Kurzai

Fonzi

et al. 2000

Molecular and Cellular Biology

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Morphological development of the fungal pathogen Candida albicans is profoundly affected by ambient pH. Acidic pH restricts growth to the yeast form, whereas neutral pH permits development of the filamentous form. Superimposed on the pH restriction is a temperature requirement of approximately 37°C for filamentation. The role of pH in development was investigated by selecting revertants of phr2⌬ mutants that had gained the ability to grow at acid pH. The extragenic suppressors in two independent revertants were identified as nonsense mutations in the pH response regulator RIM101 (PRR2) that resulted in a carboxy-terminal truncation of the open reading frame. These dominant active alleles conferred the ability to filament at acidic pH, to express PHR1, an alkaline-expressed gene, at acidic pH, and to repress the acid-expressed gene PHR2. It was also observed that both the wild-type and mutant alleles could act as multicopy suppressors of the temperature restriction on filamentation, allowing extensive filamentation at 29°C. The ability of the activated alleles to promote filamentation was dependent upon the developmental regulator EFG1. The results suggest that RIM101 is responsible for the pH dependence of hyphal development.

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Section: Discussionmentioning

confidence: 99%

Dominant Active Alleles of RIM101(PRR2) Bypass the pH Restriction on Filamentation of Candida albicans

Barkani

Kurzai

Fonzi

et al. 2000

Molecular and Cellular Biology

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“…RIM101p is a positive regulator of meiosis in budding yeast, through its stimulation of transcription of IME1, a gene encoding a key positive-acting transcription factor which activates a number of meiotic genes, including the kinase-encoding gene IME2 (117,118). Nonallelic, recessive rim101, rim8, rim9, and rim13 mutations result in a similar phenotype, characterized by reduced expression of ime1::HIS3 and ime2::lacZ gene fusions, cryosensitive growth, and smooth colony morphology (117, 118).…”

Section: Molecular Characterization Of the Rim Regulatory Systemmentioning

confidence: 99%

Regulation of Gene Expression by Ambient pH in Filamentous Fungi and Yeasts

Peñalva

Arst

2002

Microbiol Mol Biol Rev

269

213

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Life, as we know it, is water based. Exposure to hydroxonium and hydroxide ions is constant and ubiquitous, and the evolutionary pressure to respond appropriately to these ions is likely to be intense. Fungi respond to their environments by tailoring their output of activities destined for the cell surface or beyond to the ambient pH. We are beginning to glimpse how they sense ambient pH and transmit this information to the transcription factor, whose roles ensure that a suitable collection of gene products will be made. Although relatively little is known about pH signal transduction itself, its consequences for the cognate transcription factor are much clearer. Intriguingly, homologues of components of this system mediating the regulation of fungal gene expression by ambient pH are to be found in the animal kingdom. The potential applied importance of this regulatory system lies in its key role in fungal pathogenicity of animals and plants and in its control of fungal production of toxins, antibiotics, and secreted enzymes

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“…The first family encodes S. cerevisiae End13/Vps4 (30) and its murine ortholog Skd1 (31) that have ϳ30% identity to this region. The second family encodes Emericella nidulans PalB (32) and its yeast and human orthologs (Rim1p and PalBH, respectively) that have ϳ25% amino acid identity to this region (33,34). We have designated this region of homology as the ESP domain (for End13, SNX15, PalB).…”

Section: Fig 2 Subcellular Distribution Of Snx15 and Snx15a In Cos7mentioning

confidence: 99%

Identification and Characterization of SNX15, a Novel Sorting Nexin Involved in Protein Trafficking

Phillips¹,

Barr²,

Haft³

et al. 2001

Journal of Biological Chemistry

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Sorting nexins are a family of phox homology domain containing proteins that are homologous to yeast proteins involved in protein trafficking. We have identified a novel 342-amino acid residue sorting nexin, SNX15, and a 252-amino acid splice variant, SNX15A. Unlike many sorting nexins, a SNX15 ortholog has not been identified in yeast or Caenorhabditis elegans. By Northern blot analysis, SNX15 mRNA is widely expressed. Although predicted to be a soluble protein, both endogenous and overexpressed SNX15 are found on membranes and in the cytosol. The phox homology domain of SNX15 is required for its membrane association and for association with the platelet-derived growth factor receptor. We did not detect association of SNX15 with receptors for epidermal growth factor or insulin. However, overexpression of SNX15 led to a decrease in the processing of insulin and hepatocyte growth factor receptors to their mature subunits. Immunofluorescence studies showed that SNX15 overexpression resulted in mislocalization of furin, the endoprotease responsible for cleavage of insulin and hepatocyte growth factor receptors. Based on our data and the existing findings with yeast orthologs of other sorting nexins, we propose that overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the trans-Golgi network.Intracellular vesicle traffic in both yeast and mammals requires the function of numerous proteins that mediate multiple processes including cargo selection, vesicle budding, and fusion of vesicles with specific targets (1-3). Sorting nexins (SNXs) 1 are a family of widely expressed proteins believed to be part of the complex molecular machinery required for protein trafficking (4). Mammalian SNXs are homologous to several yeast proteins (e.g. Vps5p, Mvp1p, and Grd19p) for which there is strong genetic evidence demonstrating a role in protein trafficking (5-7). SNX1 was identified using the yeast two-hybrid system by virtue of its ability to bind to the cytoplasmic domain of the epidermal growth factor (EGF) receptor (8). Subsequently, SNX1 was shown to also interact with receptors for insulin, platelet-derived growth factor (PDGF), transferrin, and leptin (4). Furthermore, SNX1 is the mammalian ortholog of Vps5p, a yeast protein that is a component of a multimeric complex (termed the "retromer complex") involved in retrograde transport of proteins from prevacuolar endosomes to the TGN (9). We have previously described three additional sorting nexins: SNX2, SNX3, and SNX4 (4); and 10 additional sorting nexins (SNX5-14) have been deposited in GenBank TM . Like SNX1, both SNX2 and SNX4 associate with various receptors. In addition, SNX1, SNX2, and SNX4 assemble into oligomeric structures (4). All 14 SNX molecules contain a phox homology (PX) domain, a conserved sequence of unknown function first identified in the p40 phox and p47 phox subunits of the NADPH oxidase complex (10). PX domains consist of ϳ100 amino acid residues, and most contain a proline-rich sequence ...

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Molecular characterization of the yeast meiotic regulatory geneRIM1

Cited by 95 publications

References 33 publications

Dominant Active Alleles of RIM101(PRR2) Bypass the pH Restriction on Filamentation of Candida albicans

Dominant Active Alleles of RIM101(PRR2) Bypass the pH Restriction on Filamentation of Candida albicans

Regulation of Gene Expression by Ambient pH in Filamentous Fungi and Yeasts

Identification and Characterization of SNX15, a Novel Sorting Nexin Involved in Protein Trafficking

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