The hydrophilic N-terminal domain complements the membrane-anchored C-terminal domain of the sensor kinase KdpD of Escherichia coli

DC FieldValueLanguage
dc.contributor.authorHeermann, R
dc.contributor.authorAltendorf, K
dc.contributor.authorJung, K
dc.date.accessioned2021-12-23T16:01:09Z-
dc.date.available2021-12-23T16:01:09Z-
dc.date.issued2000
dc.identifier.issn00219258
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4790-
dc.description.abstractThe putative turgor sensor KdpD is characterized by a large, N-terminal domain of about 400 amino acids, which is not found in any other known sensor kinase. Comparison of 12 KdpD sequences from various microorganisms reveals that this part of the kinase is highly conserved and includes two motifs (Walker A and Walker B) that are very similar to the classical ATP-binding sites of ATP-requiring enzymes. By means of photoaffinity labeling with 8-azido-[alpha-P-32]ATP, direct evidence was obtained for the existence of an ATP-binding site located in the N-terminal domain of KdpD. The N-terminal domain, KdpD/1-395, was overproduced and purified. Although predicted to be hydrophilic, it was found to be membrane-associated and could be solubilized either by treatment with buffer of low ionic strength or detergent. The membrane-associated form, but not the solubilized one, retained the ability to bind 8-azido-[alpha-P-32]ATP. Previously, it was shown that the phosphatase activity of a truncated KdpD, KdpD/Delta 12-395, is deregulated in vitro (Jung, K., and Altendorf, K. (1998) J. Biol. Chem. 273, 17406-17410). Here, we demonstrated that this effect was reversed in vesicles containing both the truncated KdpD and the N-terminal domain. Furthermore, coexpression of kdpD/Delta 12-395 and kdpD/1-395 restored signal transduction in vivo. These results highlight the importance of the N-terminal domain for the function of KdpD and provide evidence for an interaction of this domain and the transmitter domain of the sensor kinase.
dc.language.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectOPERON EXPRESSION
dc.subjectPHOSPHATASE-ACTIVITY
dc.subjectPOTASSIUM
dc.subjectPRESSURE
dc.subjectPROTEIN
dc.subjectSEQUENCES
dc.subjectSIGNAL
dc.subjectSYSTEM
dc.subjectTRANSPORT
dc.subjectTURGOR SENSOR
dc.titleThe hydrophilic N-terminal domain complements the membrane-anchored C-terminal domain of the sensor kinase KdpD of Escherichia coli
dc.typejournal article
dc.identifier.doi10.1074/jbc.M000093200
dc.identifier.isiISI:000087392200095
dc.description.volume275
dc.description.issue22
dc.description.startpage17080
dc.description.endpage17085
dc.contributor.orcid0000-0003-0631-6156
dc.contributor.researcheridE-1793-2013
dc.identifier.eissn1083351X
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.netidAlKa770-
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