F-1-ATPase, the C-terminal end of subunit gamma is not required for ATP hydrolysis-driven rotation
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Muller, M | |
dc.contributor.author | Panke, O | |
dc.contributor.author | Junge, W | |
dc.contributor.author | Engelbrecht, S | |
dc.date.accessioned | 2021-12-23T16:00:33Z | - |
dc.date.available | 2021-12-23T16:00:33Z | - |
dc.date.issued | 2002 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/4458 | - |
dc.description.abstract | ATP hydrolysis by the isolated F-1-ATPase drives the rotation of the central shaft, subunit gamma, which is located within a hexagon formed by subunits (alphabeta)(3). The C-terminal end of gamma forms an alpha-helix which properly fits into the ``hydrophobic bearing'' provided by loops of subunits alpha and beta. This ``bearing'' is expected to be essential for the rotary function. We checked the importance of this contact region by successive C-terminal deletions of 3, 6, 9, 12, 15, and 18 amino acid residues (Escherichia coli F-1-ATPase). The ATP hydrolysis activity of a load-free ensemble of F-1 with 12 residues deleted decreased to 24%, of the control. EF1 with deletions of 15 or 18 residues was inactive, probably because it failed to assemble. The average torque generated by a single molecule of EF1 when loaded by a fluorescent actin filament was, however, unaffected by deletions of up to 12 residues, as was their rotational behavior (all samples rotated during 60 /- 19% of the observation time). Activation energy analysis with the ensemble revealed a moderate decrease from 54 kJ/mol for EF1 (full-length gamma) to 34 kJ/mol for EF1(gamma-12). These observations imply that the intactness of the C terminus of subunit gamma provides structural stability and/or routing during assembly of the enzyme, but that it is not required for the rotary action under load, proper. | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | BETA-SUBUNIT | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CATALYSIS | |
dc.subject | ESCHERICHIA-COLI F1-ATPASE | |
dc.subject | NONCATALYTIC SITES | |
dc.subject | ROTARY F-ATPASE | |
dc.subject | SITE-DIRECTED MUTAGENESIS | |
dc.subject | SYNTHASE | |
dc.subject | TORQUE | |
dc.subject | TRANSPORT | |
dc.subject | VISCOELASTIC DYNAMICS | |
dc.title | F-1-ATPase, the C-terminal end of subunit gamma is not required for ATP hydrolysis-driven rotation | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M201998200 | |
dc.identifier.isi | ISI:000176475700029 | |
dc.description.volume | 277 | |
dc.description.issue | 26 | |
dc.description.startpage | 23308 | |
dc.description.endpage | 23313 | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | hybrid | |
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