F-ATPase: specific observation of the rotating c subunit oligomer of EFoEF1
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Panke, O | |
dc.contributor.author | Gumbiowski, K | |
dc.contributor.author | Junge, W | |
dc.contributor.author | Engelbrecht, S | |
dc.date.accessioned | 2021-12-23T15:56:59Z | - |
dc.date.available | 2021-12-23T15:56:59Z | - |
dc.date.issued | 2000 | |
dc.identifier.issn | 00145793 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/2646 | - |
dc.description.abstract | The rotary motion in response to ATP hydrolysis of the ring of c subunits of the membrane portion, F-o, of ATP synthase, FoF1, is still under contention. It mas studied with EFoEF1 (Escherichia coli) using microvideograph 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. EFoEF1 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 mu m(2) size, in same cases yielding a proportion of 5% rotating over total filaments. The rotation mas 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. (C) 2000 Federation of European Biochemical Societies. | |
dc.language.iso | en | |
dc.publisher | ELSEVIER SCIENCE BV | |
dc.relation.ispartof | FEBS LETTERS | |
dc.subject | ATP synthase | |
dc.subject | BETA-SUBUNIT | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biophysics | |
dc.subject | Cell Biology | |
dc.subject | CROSS-LINKING | |
dc.subject | DIRECTED MUTAGENESIS | |
dc.subject | EFoEF1 | |
dc.subject | ELASTIC ENERGY | |
dc.subject | EPSILON-SUBUNIT | |
dc.subject | ESCHERICHIA-COLI F1-ATPASE | |
dc.subject | F-1-ATPASE | |
dc.subject | GAMMA-SUBUNIT | |
dc.subject | PURIFICATION | |
dc.subject | rotation | |
dc.subject | single molecule | |
dc.subject | subunit c | |
dc.subject | SYNTHASE | |
dc.title | F-ATPase: specific observation of the rotating c subunit oligomer of EFoEF1 | |
dc.type | journal article | |
dc.identifier.doi | 10.1016/S0014-5793(00)01436-8 | |
dc.identifier.isi | ISI:000086731200008 | |
dc.description.volume | 472 | |
dc.description.issue | 1 | |
dc.description.startpage | 34 | |
dc.description.endpage | 38 | |
dc.publisher.place | PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS | |
dcterms.isPartOf.abbreviation | FEBS Lett. | |
dcterms.oaStatus | Bronze | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | JuWo587 | - |
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geprüft am 19.05.2024