RapamycinFungusV1, Main, Exploration, bibRecord, 001637

Formalin can alter the intracellular localization of some transcription factors in Saccharomyces cerevisiae.

Identifieur interne : 001637 ( Main/Exploration ); précédent : 001636; suivant : 001638

Formalin can alter the intracellular localization of some transcription factors in Saccharomyces cerevisiae.

Auteurs : Jennifer J. Tate [États-Unis] ; Terrance G. Cooper

Source :

FEMS yeast research [ 1567-1356 ] ; 2008.

RBID : pubmed:19054131

Descripteurs français

KwdFr :
- Antifongiques (pharmacologie), Azote (métabolisme), Cytoplasme (métabolisme), Facteurs de transcription (métabolisme), Facteurs de transcription GATA (métabolisme), Fixateurs (pharmacologie), Formaldéhyde (pharmacologie), Microscopie de fluorescence (méthodes), Noyau de la cellule (métabolisme), Pression osmotique (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de répression (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie).
MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Azote, Cytoplasme, Facteurs de transcription, Facteurs de transcription GATA, Noyau de la cellule, Protéines de Saccharomyces cerevisiae, Protéines de répression, Saccharomyces cerevisiae.
- méthodes : Microscopie de fluorescence.
- pharmacologie : Antifongiques, Fixateurs, Formaldéhyde, Sirolimus.
- Pression osmotique, Régulation de l'expression des gènes fongiques.

English descriptors

KwdEn :
- Antifungal Agents (pharmacology), Cell Nucleus (metabolism), Cytoplasm (metabolism), Fixatives (pharmacology), Formaldehyde (pharmacology), GATA Transcription Factors (metabolism), Gene Expression Regulation, Fungal (MeSH), Microscopy, Fluorescence (methods), Nitrogen (metabolism), Osmotic Pressure (MeSH), Repressor Proteins (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Transcription Factors (metabolism).
MESH :
- chemical , genetics : Saccharomyces cerevisiae Proteins.
- chemical , metabolism : GATA Transcription Factors, Nitrogen, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Fixatives, Formaldehyde, Sirolimus.
- drug effects : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Cytoplasm, Saccharomyces cerevisiae.
- methods : Microscopy, Fluorescence.
- Gene Expression Regulation, Fungal, Osmotic Pressure.

Abstract

Indirect immunofluorescence (IF) microscopy is a frequently used method to determine intracellular protein localization. It is especially useful for low abundance proteins, for example the GATA-factors (Gln3, Gat1) which activate nitrogen catabolite repression (NCR)-sensitive transcription. Limiting nitrogen or treating cells with Tor pathway inhibitor, rapamycin, elicits nuclear GATA-factor localization and increased NCR-sensitive transcription, whereas excess nitrogen restricts these proteins to the cytoplasm and decreases transcription. The initial step of the IF procedure is formalin-fixation that quenches cellular activity and fixes protein locations via cross-linking. We find that under some conditions, formalin itself can influence GATA-factor localization. With low formalin (0.8% or 1.6%), Gat1-Myc(13) became more nuclear, and with higher concentrations (5.6%), it became more cytoplasmic. Gln3-Myc(13) localization, on the other hand, did not respond to low formalin, but became more cytoplasmic at the higher concentration. Interestingly, the high concentration of formalin had no demonstrable effect when the GATA factors were completely nuclear, i.e. after rapamycin (Gat1-Myc(13)) or Msx (Gln3-Myc(13)) treatment. These effects are most likely elicited by polyoxymethylene glycols, which significantly increase the osmolarity of the medium (0.5-2). We suggest that varying degrees of osmotic stress and transcription factor movement in response to it can occur after the beginning of fixation but before proteins become immobilized.

DOI: 10.1111/j.1567-1364.2008.00441.x
PubMed: 19054131
PubMed Central: PMC2649679

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Indirect immunofluorescence (IF) microscopy is a frequently used method to determine intracellular protein localization. It is especially useful for low abundance proteins, for example the GATA-factors (Gln3, Gat1) which activate nitrogen catabolite repression (NCR)-sensitive transcription. Limiting nitrogen or treating cells with Tor pathway inhibitor, rapamycin, elicits nuclear GATA-factor localization and increased NCR-sensitive transcription, whereas excess nitrogen restricts these proteins to the cytoplasm and decreases transcription. The initial step of the IF procedure is formalin-fixation that quenches cellular activity and fixes protein locations via cross-linking. We find that under some conditions, formalin itself can influence GATA-factor localization. With low formalin (0.8% or 1.6%), Gat1-Myc(13) became more nuclear, and with higher concentrations (5.6%), it became more cytoplasmic. Gln3-Myc(13) localization, on the other hand, did not respond to low formalin, but became more cytoplasmic at the higher concentration. Interestingly, the high concentration of formalin had no demonstrable effect when the GATA factors were completely nuclear, i.e. after rapamycin (Gat1-Myc(13)) or Msx (Gln3-Myc(13)) treatment. These effects are most likely elicited by polyoxymethylene glycols, which significantly increase the osmolarity of the medium (0.5-2). We suggest that varying degrees of osmotic stress and transcription factor movement in response to it can occur after the beginning of fixation but before proteins become immobilized.</div>
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<Abstract><AbstractText>Indirect immunofluorescence (IF) microscopy is a frequently used method to determine intracellular protein localization. It is especially useful for low abundance proteins, for example the GATA-factors (Gln3, Gat1) which activate nitrogen catabolite repression (NCR)-sensitive transcription. Limiting nitrogen or treating cells with Tor pathway inhibitor, rapamycin, elicits nuclear GATA-factor localization and increased NCR-sensitive transcription, whereas excess nitrogen restricts these proteins to the cytoplasm and decreases transcription. The initial step of the IF procedure is formalin-fixation that quenches cellular activity and fixes protein locations via cross-linking. We find that under some conditions, formalin itself can influence GATA-factor localization. With low formalin (0.8% or 1.6%), Gat1-Myc(13) became more nuclear, and with higher concentrations (5.6%), it became more cytoplasmic. Gln3-Myc(13) localization, on the other hand, did not respond to low formalin, but became more cytoplasmic at the higher concentration. Interestingly, the high concentration of formalin had no demonstrable effect when the GATA factors were completely nuclear, i.e. after rapamycin (Gat1-Myc(13)) or Msx (Gln3-Myc(13)) treatment. These effects are most likely elicited by polyoxymethylene glycols, which significantly increase the osmolarity of the medium (0.5-2). We suggest that varying degrees of osmotic stress and transcription factor movement in response to it can occur after the beginning of fixation but before proteins become immobilized.</AbstractText>
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Formalin can alter the intracellular localization of some transcription factors in Saccharomyces cerevisiae.

Formalin can alter the intracellular localization of some transcription factors in Saccharomyces cerevisiae.

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