Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli

DC FieldValueLanguage
dc.contributor.authorGassel, M
dc.contributor.authorSiebers, A
dc.contributor.authorEpstein, W
dc.contributor.authorAltendorf, K
dc.date.accessioned2021-12-23T16:12:28Z-
dc.date.available2021-12-23T16:12:28Z-
dc.date.issued1998
dc.identifier.issn00052736
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10233-
dc.description.abstractKdp, the high affinity ATP-driven K+-transport system of Escherichia coli, is a complex of the membrane-bound subunits KdpA, KdpB, KdpC and the small peptide KdpF. The assembly of this complex was studied by the analysis of mutants that expressed two of the three large subunits and inserted them into the cytoplasmic membrane. In the strains that do not express KdpC or KdpA the other two subunits did not copurify on dye-ligand affinity columns after solubilization with non-ionic detergent. In the mutant lacking KdpB the other two subunits copurified under the same conditions. It is concluded that KdpC forms strong interactions with the KdpA subunit, serving to assemble and stabilise the Kdp complex. A structure in which KdpC could be one of the connecting links between the energy-delivering subunit KdpB and the K+-transporting subunit KdpA is suggested by these data. (C) 1998 Elsevier Science B.V. All rights reserved.
dc.description.sponsorshipNIGMS NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [GM 22323] Funding Source: Medline; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM022323] Funding Source: NIH RePORTER
dc.language.isoen
dc.publisherELSEVIER SCIENCE BV
dc.relation.ispartofBIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
dc.subjectamber mutation
dc.subjectassembly
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectEXPRESSION
dc.subjectKdp-ATPase
dc.subjectOPERON
dc.subjectPROTEINS
dc.subjectPURIFICATION
dc.subjectsubunit interaction
dc.titleAssembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli
dc.typejournal article
dc.identifier.doi10.1016/S0005-2736(98)00179-5
dc.identifier.isiISI:000077781500007
dc.description.volume1415
dc.description.issue1
dc.description.startpage77
dc.description.endpage84
dc.identifier.eissn00063002
dc.publisher.placePO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
dcterms.isPartOf.abbreviationBiochim. Biophys. Acta-Biomembr.
dcterms.oaStatusBronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidAlKa770-
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