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
Creator
Uyama Taro
Kanamori Kan
Michibata Hitoshi
Source Title
Marine biotechnology
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.
Keywords
ascidian
metal accumulation
vacuolar H+-ATPase
vacuolre
gene expression
NDC
Biology [ 460 ]
Language
eng
Resource Type journal article
Publisher
Springer
Date of Issued 2001
Rights
Copyright (c) 2001 Springer "The original publication is available at www.springerlink.com"
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 isVersionOf