| Saccharomyces cerevisiae glucose signalling regulator Mth1p regulates the organellar Na+/H+ exchanger Nhx1p. | |
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MedLine Citation:
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PMID: 20858221 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Organelle-localized NHEs (Na+/H+ exchangers) are found in cells from yeast to humans and contribute to organellar pH regulation by exporting H+ from the lumen to the cytosol coupled to an H+ gradient established by vacuolar H+-ATPase. The mechanisms underlying the regulation of organellar NHEs are largely unknown. In the present study, a yeast two-hybrid assay identified Mth1p as a new binding protein for Nhx1p, an organellar NHE in Saccharomyces cerevisiae. It was shown by an in vitro pull-down assay that Mth1p bound to the hydrophilic C-terminal half of Nhx1p, especially to the central portion of this region. Mth1p is known to bind to the cytoplasmic domain of the glucose sensor Snf3p/Rgt2p and also functions as a negative transcriptional regulator. Mth1p was expressed in cells grown in a medium containing galactose, but was lost (possibly degraded) when cells were grown in medium containing glucose as the sole carbon source. Deletion of the MTH1 gene increased cell growth compared with the wild-type when cells were grown in a medium containing galactose and with hygromycin or at an acidic pH. This resistance to hygromycin or acidic conditions was not observed for cells grown with glucose as the sole carbon source. Gene knockout of NHX1 increased the sensitivity to hygromycin and acidic pH. The increased resistance to hygromycin was reproduced by truncation of the Mth1p-binding region in Nhx1p. These results implicate Mth1p as a novel regulator of Nhx1p that responds to specific extracellular carbon sources. |
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Authors:
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Keiji Mitsui; Masafumi Matsushita; Hiroshi Kanazawa |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 432 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-15 Completed Date: 2010-12-30 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 343-52 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, Graduate School of Science, Osaka University 1-1 Machikaneyama-cho, Toyonaka City, Osaka 560-0043, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing
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chemistry,
deficiency,
genetics,
metabolism* Base Sequence DNA Primers Escherichia coli / genetics Gene Expression Regulation, Fungal Gene Knockout Techniques Homeostasis Humans Immunoblotting Organelles / metabolism* Plasmids / genetics Recombinant Fusion Proteins / metabolism Recombinant Proteins / metabolism Saccharomyces cerevisiae / genetics, metabolism* Saccharomyces cerevisiae Proteins / chemistry, genetics, metabolism* Sodium-Hydrogen Antiporter / chemistry, genetics, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/DNA Primers; 0/MTH1 protein, S cerevisiae; 0/Recombinant Fusion Proteins; 0/Recombinant Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Sodium-Hydrogen Antiporter |
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