The KDP ATPase of <i>Escherichia coli</i><sup>a</sup>

Altendorf, Karlheinz; Siebers, Annette; Epstein, Wolfgang

doi:10.1111/j.1749-6632.1992.tb43799.x

Cited by 89 publications

(93 citation statements)

References 56 publications

(21 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The phosphorylation of the sensor kinase KdpD and the transfer of the phosphate group to the response regulator KdpE has been shown in vitro using membraneskytoplasmic fractions of overproducing strains (Nakashima et al, 1992; also mentioned in Altendorf et al, 1992;Siebers and Altendorf, 1992) and with a truncated soluble form of KdpD and purified KdpE (Nakashima et a]., 1993). Here we demonstrate that phosphorylation can even be detected at the level of the chromosome-encoded KdpD protein.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli

Voelkner

Puppe

Altendorf

1993

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

KdpD and KdpE, proteins that control expression of the kdpFABC operon, are members of the class of sensor kinase/response regulator proteins. Using polyclonal antibodies raised against the KdpD protein, we have been able to identify and to localize the chromosome‐encoded KdpD protein in the cytoplasmic membrane of Escherichia coli. Furthermore, it has been possible to detect differences in the expression of the KdpD protein according to the K+ concentration in the growth medium. The phosphorylation capacity of the plasmid‐encoded KdpD protein and the phospho‐transfer to KdpE was investigated. We found that both reactions were strictly dependent on the ionic conditions of the assay medium. Based on optimized conditions, we were able to detect phosphorylation of the chromosome‐encoded KdpD protein. Furthermore, replacement of the conserved histidine (His673), the predicted phosphorylation site in KdpD, by glutamine revealed that phosphorylation of KdpD was no longer possible.

show abstract

Section: Discussionmentioning

confidence: 99%

“…The kdp regulon consists of six genes, five of which are required for Kdp activity. The kdpFABC operon (Hesse et al, 1984;Altendorf et al, 1992) codes for the three membrane-bound subunits KdpA, KdpB and KdpC of the Kdp-ATPase (Laimins et al, 1978). Furthermore, an open reading frame, kdpF, of unknown function has been recognized ).…”

mentioning

confidence: 99%

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli

Voelkner

Puppe

Altendorf

1993

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…KdpA and KdpB of Synechocystis have the same predicted secondary transmembrane structure as the E. coli subunits. KdpC (Slr1730), which is present in the plasma membrane (spot 44) of Synechocystis, also has the same predicted secondary structure as the E. coli counterpart with one transmembrane helix in the amino-terminal end anchored in the plasma membrane exposing the C terminus to the cytoplasm (61).…”

Section: Table I Proteins Identified In Plasma Membranes Of Synechocymentioning

confidence: 99%

Proteomics of Synechocystis sp. Strain PCC 6803

Huang

Parmryd

Nilsson

et al. 2002

Molecular & Cellular Proteomics

162

View full text Add to dashboard Cite

Cyanobacteria are unique prokaryotes since they in addition to outer and plasma membranes contain the photosynthetic membranes (thylakoids). The plasma membranes of Synechocystis 6803, which can be completely purified by density centrifugation and polymer two-phase partitioning, have been found to be more complex than previously anticipated, i.e. they appear to be essential for assembly of the two photosystems. A proteomic approach for the characterization of cyanobacterial plasma membranes using two-dimensional gel electrophoresis and mass spectrometry analysis revealed a total of 57 different membrane proteins of which 17 are integral membrane spanning proteins. Among the 40 peripheral proteins 20 are located on the periplasmic side of the membrane, while 20 are on the cytoplasmic side. Among the proteins identified are subunits of the two photosystems as well as Vipp1, which has been suggested to be involved in vesicular transport between plasma and thylakoid membranes and is thus relevant to the possibility that plasma membranes are the initial site for photosystem biogenesis. Four subunits of the Pilus complex responsible for cell motility were also identified as well as several subunits of the TolC and TonB transport systems. Several periplasmic and ATP-binding proteins of ATPbinding cassette transporters were also identified as were two subunits of the F 0 membrane part of the ATP synthase.

show abstract

“…

7).The number of identified P-type ATPases is growing rapidly. In the course of cloning other genes from Synechococcus 7942, we found one that appears to encode a P-type ATPase.

…”

mentioning

confidence: 99%

P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products.

Phung

Ajlani

Haselkorn

1994

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

7).The number of identified P-type ATPases is growing rapidly. In the course of cloning other genes from Synechococcus 7942, we found one that appears to encode a P-type ATPase. During the preparation of this paper three other cyanobacterial P-type ATPase sequences were published (8, 9). The first of these new reports concerns two genes for P-type ATPases from the same Synechococcus strain used in this study (8). However, the sequences of these genes differ significantly from the one we describe here. In addition, biochemical evidence indicates that the Synechococcus plasma membrane contains a P-type ATPase (10).We (Pharmacia), was selected on plates containing kanamycin at 50 ug/ml. For selective growth of E. coli strain DH5a (GIBCO/BRL) carrying antibiotic-resistance plasmids, ampicillin at 100 pug/ml or tetracycline 12 pig/ml was used.Cloning and Sequence Determination. Standard molecular genetic techniques, including DNA isolation, restriction nuclease digestion and ligation, and Southern and Northern blotting, were as described by Sambrook et al. (13). Genomic DNA was prepared from cells of Synechococcus 7942 according to Brusslan (14). RNA isolation was as described by Schaefer and Golden (15). A fragment containing part of the ctaA gene was isolated from a two-step size-fractionated Synechococcus DNA library. Synechococcus genomic DNA was first digested with BamHI and the restriction fiagments were separated by electrophoresis in an agarose gel. Fragments of 3-6 kb were isolated and digested with HindIII. Fragments of 2-3 kb were isolated, cloned into plasmid pBR322, and transformed into E. coli strain DH5a. Clone pLP180 (containing a 2.6-kb HindIII-BamHI fiagment) was identified by screening individual plasmid DNAs with an E. coli fabE (16) fragment as probe. A 320-bp Pst I-BamHI fragment was isolated from the HindIII-BamHI insert of pLP180 and used as probe to screen a library of wild-type Synechococcus genomic DNA in the cosmid vector pWB79 (prepared by J. Brusslan, University of Chicago). A 7-kb HindIll fragment was identified and smaller restriction nuclease fragments from it were subcloned into pUC18 and pBluescript vectors (Stratagene).Subclones for sequencing were generated either by nested deletion using the Erase-a-base kit (Promega) or by digesting the original clones with appropriate restriction nucleases and religating. Sequencing was done on both strands by the dideoxy chain-termination method with Sequenase version 2.0 (United States Biochemical) with either M13 universal and reverse primers or synthetic oligonucleotide primers. Fig. 1 summarizes the physical map of the 7-kb HindIII fragment and the 4.5-kb HindIII-EcoRV region within it that was sequenced completely on both strands.Insertional Inactivation of the ctaA Gene. The kanamycinresistance cassette from pUC4K was inserted between the Bgl II and Pst I sites of pLP1.5 (a pUC18-derived plasmid

show abstract

The KDP ATPase of Escherichia coli^a

Cited by 89 publications

References 56 publications

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli

Proteomics of Synechocystis sp. Strain PCC 6803

P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products.

Contact Info

Product

Resources

About

The KDP ATPase of Escherichia colia

Cited by 89 publications

References 56 publications

Characterization of the KdpD protein, the sensor kinase of the K+‐translocating Kdp system of Escherichia coli

Characterization of the KdpD protein, the sensor kinase of the K+‐translocating Kdp system of Escherichia coli

Proteomics of Synechocystis sp. Strain PCC 6803

P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products.

Contact Info

Product

Resources

About

The KDP ATPase of Escherichia coli^a

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli

Characterization of the KdpD protein, the sensor kinase of the K⁺‐translocating Kdp system of Escherichia coli