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| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C0042219 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C0018437 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:16891312 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16891312 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:16891312 | pubmed:dateCreated | 2006-10-2 | lld:pubmed |
| pubmed-article:16891312 | pubmed:abstractText | Vacuolar proton-translocating ATPase pumps consist of two domains, V(1) and V(o). Subunit d is a component of V(o) located in a central stalk that rotates during catalysis. By generating mutations, we showed that subunit d couples ATP hydrolysis and proton transport. The mutation F94A strongly uncoupled the enzyme, preventing proton transport but not ATPase activity. C-terminal mutations changed coupling as well; ATPase activity was decreased by 59-72%, whereas proton transport was not measurable (E328A) or was moderately reduced (E317A and C329A). Except for W325A, which had low levels of V(1)V(o), mutations allowed wild-type assembly regardless of the fact that subunits E and d were reduced at the membrane. N- and C-terminal deletions of various lengths were inhibitory and gradually destabilized subunit d, limiting V(1)V(o) formation. Both N and C terminus were required for V(o) assembly. The N-terminal truncation 2-19Delta prevented V(1)V(o) formation, although subunit d was available. The C terminus was required for retention of subunits E and d at the membrane. In addition, the C terminus of its bacterial homolog (subunit C from T. thermophilus) stabilized the yeast subunit d mutant 310-345Delta and allowed assembly of the rotor structure with subunits A and B. Structural features conserved between bacterial and eukaryotic subunit d and the significance of domain 3 for vacuolar proton-translocating ATPase function are discussed. | lld:pubmed |
| pubmed-article:16891312 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16891312 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16891312 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16891312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16891312 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16891312 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16891312 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:OwegiMargaret... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:BilboSarah... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:PappasDonald... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:FinchMark... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:ResendizCruz... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:JacqueminLori... | lld:pubmed |
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| pubmed-article:16891312 | pubmed:author | pubmed-author:McCullochKath... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:MargalefKatri... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:MertzMelissa... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:StormsJason... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:DaminCraig... | lld:pubmed |
| pubmed-article:16891312 | pubmed:author | pubmed-author:ParraKarlett... | lld:pubmed |
| pubmed-article:16891312 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16891312 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:16891312 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16891312 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16891312 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16891312 | pubmed:pagination | 30001-14 | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:meshHeading | pubmed-meshheading:16891312... | lld:pubmed |
| pubmed-article:16891312 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16891312 | pubmed:articleTitle | Identification of a domain in the V0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase. | lld:pubmed |
| pubmed-article:16891312 | pubmed:affiliation | Department of Chemistry, Ball State University, Muncie, Indiana 47306, USA. | lld:pubmed |
| pubmed-article:16891312 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16891312 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16891312 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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