| pubmed-article:10781800 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10781800 | lifeskim:mentions | umls-concept:C0302523 | lld:lifeskim |
| pubmed-article:10781800 | lifeskim:mentions | umls-concept:C0700325 | lld:lifeskim |
| pubmed-article:10781800 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:10781800 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:10781800 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:10781800 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10781800 | pubmed:dateCreated | 2000-6-2 | lld:pubmed |
| pubmed-article:10781800 | pubmed:abstractText | The rotary motion in response to ATP hydrolysis of the ring of c subunits of the membrane portion, F(o), of ATP synthase, F(o)F(1), is still under contention. It was studied with EF(o)EF(1) (Escherichia coli) using microvideography with a fluorescent actin filament. To overcome the limited specificity of actin attachment through a Cys-maleimide couple which might have hampered the interpretation of previous work, we engineered a 'strep-tag' sequence into the C-terminal end of subunit c. It served (a) to purify the holoenzyme and (b) to monospecifically attach a fluorescent actin filament to subunit c. EF(o)EF(1) was immobilized on a Ni-NTA-coated glass slide by the engineered His-tag at the N-terminus of subunit beta. In the presence of MgATP we observed up to five counterclockwise rotating actin filaments per picture frame of 2000 microm(2) size, in some cases yielding a proportion of 5% rotating over total filaments. The rotation was unequivocally attributable to the ring of subunit c. The new, doubly engineered construct serves as a firmer basis for ongoing studies on torque and angular elastic distortions between F(1) and F(o). | lld:pubmed |
| pubmed-article:10781800 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10781800 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781800 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10781800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10781800 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10781800 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10781800 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10781800 | pubmed:author | pubmed-author:JungeWW | lld:pubmed |
| pubmed-article:10781800 | pubmed:author | pubmed-author:EngelbrechtSS | lld:pubmed |
| pubmed-article:10781800 | pubmed:author | pubmed-author:PänkeOO | lld:pubmed |
| pubmed-article:10781800 | pubmed:author | pubmed-author:GumbiowskiKK | lld:pubmed |
| pubmed-article:10781800 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10781800 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:10781800 | pubmed:volume | 472 | lld:pubmed |
| pubmed-article:10781800 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10781800 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10781800 | pubmed:pagination | 34-8 | lld:pubmed |
| pubmed-article:10781800 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10781800 | pubmed:meshHeading | pubmed-meshheading:10781800... | lld:pubmed |
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| pubmed-article:10781800 | pubmed:meshHeading | pubmed-meshheading:10781800... | lld:pubmed |
| pubmed-article:10781800 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10781800 | pubmed:articleTitle | F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1). | lld:pubmed |
| pubmed-article:10781800 | pubmed:affiliation | Universität Osnabrück, Fachbereich Biologie, Abteilung Biophysik, Barbarastr. 11, 49069, Osnabrück, Germany. | lld:pubmed |
| pubmed-article:10781800 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10781800 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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