The transmembrane domain of subunit b of the Escherichia coli F1F0 ATP synthase is sufficient for H+-translocating activity together with subunits a and c
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Greie, JC | |
dc.contributor.author | Heitkamp, T | |
dc.contributor.author | Altendorf, K | |
dc.date.accessioned | 2021-12-23T15:56:24Z | - |
dc.date.available | 2021-12-23T15:56:24Z | - |
dc.date.issued | 2004 | |
dc.identifier.issn | 00142956 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/2331 | - |
dc.description.abstract | Subunit b is indispensable for the formation of a functional H+-translocating F-O complex both in vivo and in vitro. Whereas the very C-terminus of subunit b interacts with F-1 and plays a crucial role in enzyme assembly, the C-terminal region is also considered to be necessary for proper reconstitution of F-O into liposomes. Here, we show that a synthetic peptide, residues 1-34 of subunit b (b(1-34)) [Dmitriev, O., Jones, P.C., Jiang, W. & Fillingame, R.H. (1999) J. Biol. Chem.274, 15598-15604], corresponding to the membrane domain of subunit b was sufficient in forming an active F-O complex when coreconstituted with purified ac subcomplex. H+ translocation was shown to be sensitive to the specific inhibitor N,N'-dicyclohexylcarbodiimide, and the resulting F-O complexes were deficient in binding of isolated F-1. This demonstrates that only the membrane part of subunit b is sufficient, as well as necessary, for H+ translocation across the membrane, whereas the binding of F-1 to F-O is mainly triggered by C-terminal residues beyond Glu34 in subunit b. Comparison of the data with former reconstitution experiments additionally indicated that parts of the hydrophilic portion of the subunit b dimer are not involved in the process of ion translocation itself, but might organize subunits a and c in F-O assembly. Furthermore, the data obtained functionally support the monomeric NMR structure of the synthetic b(1-34). | |
dc.language.iso | en | |
dc.publisher | BLACKWELL PUBLISHING LTD | |
dc.relation.ispartof | EUROPEAN JOURNAL OF BIOCHEMISTRY | |
dc.subject | 2ND STALK | |
dc.subject | BINDING | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CROSS-LINKING | |
dc.subject | DELTA-SUBUNIT | |
dc.subject | EPSILON-SUBUNIT | |
dc.subject | Escherichia coli | |
dc.subject | F-0 COMPLEX | |
dc.subject | F1FO ATP synthase | |
dc.subject | ORGANIZATION | |
dc.subject | PROTEINS | |
dc.subject | proton translocation | |
dc.subject | RECONSTITUTION | |
dc.subject | subunit b | |
dc.subject | TRANSPORT | |
dc.title | The transmembrane domain of subunit b of the Escherichia coli F1F0 ATP synthase is sufficient for H+-translocating activity together with subunits a and c | |
dc.type | journal article | |
dc.identifier.doi | 10.1111/j.1432-1033.2004.04235.x | |
dc.identifier.isi | ISI:000222419200019 | |
dc.description.volume | 271 | |
dc.description.issue | 14 | |
dc.description.startpage | 3036 | |
dc.description.endpage | 3042 | |
dc.publisher.place | 9600 GARSINGTON RD, OXFORD OX4 2DG, OXON, ENGLAND | |
dcterms.isPartOf.abbreviation | Eur. J. Biochem. | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | AlKa770 | - |
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