| pubmed-article:8016125 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0042219 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0034318 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C1159576 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:8016125 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:8016125 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8016125 | pubmed:dateCreated | 1994-7-28 | lld:pubmed |
| pubmed-article:8016125 | pubmed:abstractText | The membrane bounding the vacuole of plant cells contains two electrogenic proton pumps. These are the vacuolar H(+)-ATPase (EC 3.6.1.3), an enzyme common to all eukaryotes, and a vacuolar H(+)-translocating pyrophosphatase (EC 3.6.1.1), which is ubiquitous in plants but otherwise known in only a few phototrophic bacteria. Although the substrate-binding subunit of the vacuolar H(+)-pyrophosphatase has been identified and purified and cDNAs encoding it have been isolated and characterized, the minimal unit competent in pyrophosphate (PPi)-energized H+ translocation is not known. Here we address this question and show that heterologous expression of the cDNA (AVP) encoding the substrate-binding subunit of the vacuolar H(+)-pyrophosphatase from the vascular plant Arabidopsis thaliana in the yeast Saccharomyces cerevisiae results in the production of vacuolarly localized functional enzyme active in PPi-dependent H+ translocation. Since the heterologously expressed pump is indistinguishable from the native plant enzyme with respect to PPi hydrolysis, H+ translocation, activation by potassium, and selective inhibition by calcium and 1,1-diphosphonates, it is concluded that all of the known catalytic functions of the enzyme map to the one subunit encoded by AVP. | lld:pubmed |
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| pubmed-article:8016125 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8016125 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8016125 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8016125 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8016125 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8016125 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8016125 | pubmed:author | pubmed-author:KimE JEJ | lld:pubmed |
| pubmed-article:8016125 | pubmed:author | pubmed-author:ReaP APA | lld:pubmed |
| pubmed-article:8016125 | pubmed:author | pubmed-author:ZhenR GRG | lld:pubmed |
| pubmed-article:8016125 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8016125 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:8016125 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:8016125 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8016125 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8016125 | pubmed:pagination | 6128-32 | lld:pubmed |
| pubmed-article:8016125 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:8016125 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8016125 | pubmed:articleTitle | Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. | lld:pubmed |
| pubmed-article:8016125 | pubmed:affiliation | Department of Biology, University of Pennsylvania, Philadelphia 19104. | lld:pubmed |
| pubmed-article:8016125 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8016125 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8016125 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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