Subunit organization of the stator part of the F-0 complex from Escherichia coli ATP synthase

DC FieldValueLanguage
dc.contributor.authorGreie, JC
dc.contributor.authorDeckers-Hebestreit, G
dc.contributor.authorAltendorf, K
dc.date.accessioned2021-12-23T16:05:20Z-
dc.date.available2021-12-23T16:05:20Z-
dc.date.issued2000
dc.identifier.issn0145479X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6923-
dc.description.abstractMembrane-bound ATP synthases (F1F0) catalyze the synthesis of ATP via a rotary catalytic mechanism utilizing the energy of an electrochemical ion gradient. The transmembrane potential is supposed to propel rotation of a subunit c ring of F-0 together with subunits gamma and epsilon of F-1, thereby forming the rotor part of the enzyme, whereas the remainder of the F1F0 complex functions as a stator for compensation of the torque generated during rotation. This review focuses on our recent work on the stator part of the F-o complex, e.g., subunits a and b. Using epitope insertion and antibody binding, subunit a was shown to comprise six transmembrane helixes with both the N- and C-terminus oriented toward the cytoplasm. By use of circular dichroism (CD) spectroscopy, the secondary structure of subunit b incorporated into proteoliposomes was determined to be 80% alpha -helical together with 14% beta turn conformation, providing flexibility to the second stalk. Reconstituted subunit b together with isolated ac subcomplex was shown to be active in proton translocation and functional F-1 binding revealing the native conformation of the polypeptide chain. Chemical crosslinking in everted membrane vesicles led to the formation of subunit b homodimers around residues bQ37 to bL65, whereas bA32C could be crosslinked to subunit a, indicating a close proximity of subunits a and b near the membrane. Further evidence for the proposed direct interaction between subunits a and b was obtained by purification of a stable ab(2) subcomplex via affinity chromatography using His tags fused to subunit a or b. This ab(2) subcomplex was shown to be active in proton translocation and F-1 binding, when coreconstituted with subunit c. Consequences of crosslink formation and subunit interaction within the F1F0 complex are discussed.
dc.language.isoen
dc.publisherKLUWER ACADEMIC/PLENUM PUBL
dc.relation.ispartofJOURNAL OF BIOENERGETICS AND BIOMEMBRANES
dc.subject2ND STALK
dc.subjectab(2) subcomplex
dc.subjectATP synthase
dc.subjectB-SUBUNIT
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectcircular dichroism
dc.subjectCROSS-LINKING
dc.subjectcrosslinking
dc.subjectDELTA-SUBUNIT
dc.subjectEPSILON-SUBUNIT
dc.subjectEscherichia coli
dc.subjectF1F0
dc.subjectF1F0-ATP SYNTHASE
dc.subjectH+-ATPASE
dc.subjectMEMBRANE-PROTEINS
dc.subjectPROTON TRANSLOCATION
dc.subjectsubunit a
dc.subjectsubunit b
dc.subjectTRANSMEMBRANE TOPOLOGY
dc.titleSubunit organization of the stator part of the F-0 complex from Escherichia coli ATP synthase
dc.typejournal article
dc.identifier.doi10.1023/A:1005523902800
dc.identifier.isiISI:000165750500006
dc.description.volume32
dc.description.issue4
dc.description.startpage357
dc.description.endpage364
dc.publisher.place233 SPRING ST, NEW YORK, NY 10013 USA
dcterms.isPartOf.abbreviationJ. Bioenerg. Biomembr.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidDeGa700-
crisitem.author.netidAlKa770-
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