Subunit C of the Vacuolar-Type ATPase from the Vanadium-Rich Ascidian, Ascidia sydneiensis samea, Rescued the pH Sensitivity of Yeast vma5 Mutants
Marine biotechnology Volume 3
Page 316-321
published_at 2001
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Title ( eng ) |
Subunit C of the Vacuolar-Type ATPase from the Vanadium-Rich Ascidian, Ascidia sydneiensis samea, Rescued the pH Sensitivity of Yeast vma5 Mutants
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Creator |
Uyama Taro
Kanamori Kan
Michibata Hitoshi
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Source Title |
Marine biotechnology
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Volume | 3 |
Start Page | 316 |
End Page | 321 |
Abstract |
A vanadium-accumulating ascidian, Ascidia sydneiensis samea, expresses vacuolar-type H+-ATPases (V ATPases) on the vacuole membrane of the vanadium-containing blood cells known as vanadocytes. Previously, we showed that the contents of their vacuoles are extremely acidic and that a V ATPase-specific inhibitor, bafilomycin A1, neutralized the contents of the vacuoles. To understand the function of V ATPase in vanadocytes, we isolated cDNA encoding subunit C of V ATPase from vanadocytes since this subunit has been known to be responsible for the assembly of V-ATPases and to regulate the ATPase activity of V-ATPases. The cloned cDNA was 1,443 nucleotides in length, and encoded a putative 384 amino-acid protein. By expressing the ascidian cDNA for subunit C under the control of a galactose-inducible promoter, the pH-sensitive phenotype of the corresponding vma5 mutant of a budding yeast was rescued. This result showed that the ascidian cDNA for subunit C functioned in yeast cells.
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Keywords |
ascidian
metal accumulation
vacuolar H+-ATPase
vacuolre
gene expression
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NDC |
Biology [ 460 ]
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Language |
eng
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Resource Type | journal article |
Publisher |
Springer
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Date of Issued | 2001 |
Rights |
Copyright (c) 2001 Springer "The original publication is available at www.springerlink.com"
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Publish Type | Author’s Original |
Access Rights | open access |
Source Identifier |
[ISSN] 1436-2228
[DOI] 10.1007/s1012601-0054-x
[PMID] 14961347
[DOI] http://dx.doi.org/10.1007/s1012601-0054-x
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