| pubmed-article:7580256 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0026339 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0018437 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C0597488 | lld:lifeskim |
| pubmed-article:7580256 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:7580256 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:7580256 | pubmed:dateCreated | 1995-12-20 | lld:pubmed |
| pubmed-article:7580256 | pubmed:abstractText | The plasma membrane proton pump (H(+)-ATPase) energizes solute uptake by secondary transporters. Wild-type Arabidopsis plasma membrane H(+)-ATPase (AHA2) and truncated H(+)-ATPase lacking 38, 51, 61, 66, 77, 92, 96, and 104 C-terminal amino acids were produced in yeast. All AHA2 species were correctly targeted to the yeast plasma membrane and, in addition, accumulated in internal membranes. Removal of 38 C-terminal residues from AHA2 produced a high-affinity state of plant H(+)-ATPase with a low Km value (0.1 mM) for ATP. Removal of an additional 12 amino acids from the C terminus resulted in a significant increase in molecular activity of the enzyme. There was a close correlation between molecular activity of the various plant H(+)-ATPase species and their ability to complement mutants of the endogenous yeast plasma membrane H(+)-ATPase (pma1). This correlation demonstrates that, at least in this heterologous host, activation of H(+)-ATPase is a prerequisite for proper energization of the plasma membrane. | lld:pubmed |
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| pubmed-article:7580256 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7580256 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7580256 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7580256 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7580256 | pubmed:issn | 1040-4651 | lld:pubmed |
| pubmed-article:7580256 | pubmed:author | pubmed-author:VillalbaJ MJM | lld:pubmed |
| pubmed-article:7580256 | pubmed:author | pubmed-author:PalmgrenM GMG | lld:pubmed |
| pubmed-article:7580256 | pubmed:author | pubmed-author:LanfermeijerF... | lld:pubmed |
| pubmed-article:7580256 | pubmed:author | pubmed-author:RegenbergBB | lld:pubmed |
| pubmed-article:7580256 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7580256 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:7580256 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7580256 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7580256 | pubmed:pagination | 1655-66 | lld:pubmed |
| pubmed-article:7580256 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:7580256 | pubmed:meshHeading | pubmed-meshheading:7580256-... | lld:pubmed |
| pubmed-article:7580256 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7580256 | pubmed:articleTitle | C-terminal deletion analysis of plant plasma membrane H(+)-ATPase: yeast as a model system for solute transport across the plant plasma membrane. | lld:pubmed |
| pubmed-article:7580256 | pubmed:affiliation | Department of Plant Biology, Royal Veterinary and Agricultural University, Copenhagen, Denmark. | lld:pubmed |
| pubmed-article:7580256 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7580256 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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