DC Element | Wert | Sprache |
dc.contributor.author | Jung, K | |
dc.contributor.author | Tjaden, B | |
dc.contributor.author | Altendorf, K | |
dc.date.accessioned | 2021-12-23T15:58:47Z | - |
dc.date.available | 2021-12-23T15:58:47Z | - |
dc.date.issued | 1997 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/3564 | - |
dc.description.abstract | In response to K+ availability or medium osmolality, the sensor kinase KdpD and the response regulator KdpE control the expression of the kdpFABC operon, coding for the high affinity K+-translocating Kdp ATPase of Escherichia coli. The stimulus for KdpD to undergo autophosphorylation is believed to be a change in turgor or some effect thereof, reflecting the role of K+ as an important cytoplasmic osmotic solute, The membrane-bound sensor kinase KdpD was overproduced as a fusion protein containing six contiguous histidine residues two amino acids before the C terminus. This KdpD-His(6), protein was functional in vitro and in vivo, KdpD-His(6) was purified from everted membrane vesicles by solubilization with the zwitterionic detergent lauryldimethylamine oxide followed by nickel chelate chromatography and ion exchange chromatography to >99% homogeneity. The solubilized protein was not active with respect to autophosphorylation, but retained the ability to bind a-azido-ATP. KdpD-His(6), was reconstituted into proteoliposomes in a unidirectional inside-out orientation as revealed by ATP accessibility and protease susceptibility. Purified and reconstituted KdpD-His(6), exhibited autokinase activity, and the phosphoryl group could be transferred to KdpE, Furthermore, KdpD-His(6), was found to be the only protein that mediates dephosphorylation of KdpE similar to P. | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | 2 REGULATORY COMPONENTS | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CONTROL EXPRESSION | |
dc.subject | DRIVEN POTASSIUM-TRANSPORT | |
dc.subject | KDPABC OPERON | |
dc.subject | KINASE-ACTIVITY | |
dc.subject | OSMOSENSOR | |
dc.subject | PHOSPHORYLATION | |
dc.subject | SIGNAL TRANSDUCTION | |
dc.subject | STRUCTURAL PROTEINS | |
dc.subject | SYSTEM | |
dc.title | Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli | |
dc.type | journal article | |
dc.identifier.isi | ISI:A1997WV26200074 | |
dc.description.volume | 272 | |
dc.description.issue | 16 | |
dc.description.startpage | 10847 | |
dc.description.endpage | 10852 | |
dc.identifier.eissn | 1083351X | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | AlKa770 | - |