DC Field | Value | Language |
dc.contributor.author | Birkenhager, R | |
dc.contributor.author | Greie, JC | |
dc.contributor.author | Altendorf, K | |
dc.contributor.author | Deckers-Hebestreit, G | |
dc.date.accessioned | 2021-12-23T15:59:33Z | - |
dc.date.available | 2021-12-23T15:59:33Z | - |
dc.date.issued | 1999 | |
dc.identifier.issn | 00142956 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/3996 | - |
dc.description.abstract | The antigenic determinants of mAbs against subunit c of the Escherichia coli ATP synthase were mapped by ELISA using overlapping synthetic heptapeptides. All epitopes recognized are located in the hydrophilic loop region and are as follows: 31-LGGKFLE-37, 35-FLEGAAR-41, 36-LEGAAR-41 and 36-LEGAARQ-42. Binding studies with membrane vesicles of different orientation revealed that all mAbs bind to everted membrane vesicles independent of the presence or absence of the F-1 part. Although the hydrophilic region of subunit c and particularly the highly conserved residues A40, R41, Q42 and P43 are known to interact with subunits gamma and epsilon of the F-1 part, the mAb molecules have no effect on the function of F-0. Furthermore, it could be demonstrated that the F-1 part and the mAb molecule(s) are bound simultaneously to the F-0 complex suggesting that not all c subunits are involved in F-1 interaction. From the results obtained, it can be concluded that this interaction is fixed, which means that subunits gamma and epsilon do not switch between the c subunits during catalysis and furthermore, a complete rotation of the subunit c oligomer modified with mAb(s) along the stator of the F1F0 complex, proposed to be composed of at least subunits b and delta, seems to be unlikely. | |
dc.language.iso | en | |
dc.publisher | WILEY-BLACKWELL | |
dc.relation.ispartof | EUROPEAN JOURNAL OF BIOCHEMISTRY | |
dc.subject | ALPHA-SUBUNIT | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CROSS-LINKING | |
dc.subject | DELTA-SUBUNIT | |
dc.subject | EPSILON-SUBUNIT | |
dc.subject | Escherichia coli | |
dc.subject | F-1 interaction | |
dc.subject | F0F1-ATPase | |
dc.subject | H+-ATPASE | |
dc.subject | H+/ATP COUPLING RATIO | |
dc.subject | monoclonal antibodies | |
dc.subject | MONOCLONAL-ANTIBODIES | |
dc.subject | POLAR LOOP REGION | |
dc.subject | POLYCLONAL ANTIBODIES | |
dc.subject | subunit c | |
dc.subject | TRANSMEMBRANE HELIX | |
dc.title | F-0 complex of the Escherichia coli ATP synthase - Not all monomers of the subunit c oligomer are involved in F-1 interaction | |
dc.type | journal article | |
dc.identifier.doi | 10.1046/j.1432-1327.1999.00652.x | |
dc.identifier.isi | ISI:000082367500014 | |
dc.description.volume | 264 | |
dc.description.issue | 2 | |
dc.description.startpage | 385 | |
dc.description.endpage | 396 | |
dc.publisher.place | 111 RIVER ST, HOBOKEN 07030-5774, NJ USA | |
dcterms.isPartOf.abbreviation | Eur. J. Biochem. | |
dcterms.oaStatus | Bronze | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | AlKa770 | - |
crisitem.author.netid | DeGa700 | - |