F-1-ATPase, the C-terminal end of subunit gamma is not required for ATP hydrolysis-driven rotation

DC FieldValueLanguage
dc.contributor.authorMuller, M
dc.contributor.authorPanke, O
dc.contributor.authorJunge, W
dc.contributor.authorEngelbrecht, S
dc.date.accessioned2021-12-23T16:00:33Z-
dc.date.available2021-12-23T16:00:33Z-
dc.date.issued2002
dc.identifier.issn00219258
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4458-
dc.description.abstractATP 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.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBETA-SUBUNIT
dc.subjectBiochemistry & Molecular Biology
dc.subjectCATALYSIS
dc.subjectESCHERICHIA-COLI F1-ATPASE
dc.subjectNONCATALYTIC SITES
dc.subjectROTARY F-ATPASE
dc.subjectSITE-DIRECTED MUTAGENESIS
dc.subjectSYNTHASE
dc.subjectTORQUE
dc.subjectTRANSPORT
dc.subjectVISCOELASTIC DYNAMICS
dc.titleF-1-ATPase, the C-terminal end of subunit gamma is not required for ATP hydrolysis-driven rotation
dc.typejournal article
dc.identifier.doi10.1074/jbc.M201998200
dc.identifier.isiISI:000176475700029
dc.description.volume277
dc.description.issue26
dc.description.startpage23308
dc.description.endpage23313
dc.publisher.place9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatushybrid
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidJuWo587-
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