Nucleotide sequence of the Rickettsia prowazekii ATP/ADP translocase-encoding gene

Williamson, L. R.; Plano, Gregory V.; Winkler, Herbert H.; Krause, Duncan C.; Wood, Douglas

doi:10.1016/0378-1119(89)90291-6

Cited by 58 publications

(44 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…To analyze the effect of site-directed mutations on the function of a protein it is advantageous to focus on amino-acid residues conserved in homologous proteins. To identify conserved amino-acid residues we compared published [13,15,16,27,28] and unpublished protein sequences from all 15 known members, plant and bacterial, of this transporter family. Although not all 15 transporters facilitate the obligatory exchange of ATP/ADP, all members whose function is known are involved in the transport of nucleotides.…”

Section: R E S U L T Smentioning

confidence: 99%

“…Neither plastidic nor bacterial types show homology to the mitochondrial ADP/ATP carriers and are insensitive to the AAC inhibitors [17]. The plastidic and bacterial ATP/ADP transporters belong to the 12 transmembrane domain family of solute transporters [13,15,18], and share with the mitochondrial family an obligatory one-forone ATP/ADP exchange mechanism. As the plastidic and bacterial nonmitochondrial adenylate transporters import cytosolic ATP, the movement of adenylates occur in a direction opposite to that catalyzed by AAC in the mitochondrial inner membrane [1,2,19,20].…”

mentioning

confidence: 99%

“…This transporter displays a high structural similarity to the third type of ATP/ADP transporter, that from rickettsiae [15] and chlamydiae [16], obligate intracellular bacteria that grow within eukaryotic cells. Neither plastidic nor bacterial types show homology to the mitochondrial ADP/ATP carriers and are insensitive to the AAC inhibitors [17].…”

mentioning

confidence: 99%

See 2 more Smart Citations

Charged amino-acid residues in transmembrane domains of the plastidic ATP/ADP transporter from Arabidopsis are important for transport efficiency, substrate specificity, and counter exchange properties

Trentmann¹,

Decker²,

Winkler³

et al. 2000

Eur J Biochem

Self Cite

View full text Add to dashboard Cite

Structure±function relationships of the plastidic ATP/ADP transporter from Arabidopsis thaliana have been determined using site-directed mutants at positions K155, E245, E385, and K527. These charged residues are found within highly conserved domains of homologous transport proteins from plants and bacteria and are located in predicted transmembrane regions. Mutants of K155 to K155E, K155R, or K155Q reduced ATP transport to values between 4 and 16% of wild-type uptake, whereas ADP transport was always less then 3% of the wild-type value. Site-directed mutations in which glutamate at positions 245 or 385 was replaced with lysine, abolished transport. However, conservative (E245D, E385D) or neutral (E245Q, E385Q) replacement at these two positions allowed transport. The fourth reciprocal exchange, K527E, also abolished uptake of both adenylates. K527R and K527Q were unable to transport ATP, but ADP transport remained at 35 and 27%, respectively, of the wild-type activity. There was a 70-fold decreased apparent affinity of K527R for ATP, but only a twofold decrease for ADP. The efflux of ATP, but not ADP, was also greatly reduced in K527R. These observations show strikingly that K527 plays a role in substrate specificity that is manifest in both the influx and efflux components of this antiporter.Keywords: ATP/ADP transporter; structure/function relationship; site-specific mutations; plastid; Arabidopsis thaliana.Transport of solutes across cellular membranes, whether catalyzed by channels or carriers, is necessary for complex metabolism. Although adenine nucleotides, the universal cellular energy currency, fulfil an irreplaceable function, they are viewed as part of the intracellular compartment and often are not transported across biological membranes. However, there are three exceptions to this generalization in which transport of ATP and ADP appropriately occurs: in obligate intracellular bacteria, in mitochondria, and in plastids.In heterotrophic eukaryotic cells, most ATP is synthesized during oxidative phosphorylation and accumulates in the mitochondrial matrix, making it necessary to export this intermediate into the cytosol to fuel anabolic reactions. This transport is mediated by the mitochondrial ADP/ATP carrier (AAC), one of the best-characterized membrane carrier proteins [1±7]. AAC is a member of a large group of transporters comprising the mitochondrial carrier family [3]. These carriers share the same evolutionary ancestor, exhibit an internal sequence triplication of about 100 amino acids, and in the functional state probably form a homodimer from the monomer that has six transmembrane domains [8±10].A second type of adenylate transporter resides in the inner envelope membrane of plant plastids [11±14]. This transporter displays a high structural similarity to the third type of ATP/ADP transporter, that from rickettsiae [15] and chlamydiae [16], obligate intracellular bacteria that grow within eukaryotic cells. Neither plastidic nor bacterial types show homology to the mitochondrial ADP/ATP carrier...

show abstract

Section: R E S U L T Smentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Charged amino-acid residues in transmembrane domains of the plastidic ATP/ADP transporter from Arabidopsis are important for transport efficiency, substrate specificity, and counter exchange properties

Trentmann¹,

Decker²,

Winkler³

et al. 2000

Eur J Biochem

Self Cite

View full text Add to dashboard Cite

show abstract

“…The amino acid sequence of the novel ATP/ADP translocator from A. thaliana (AATP1) and the ATP/ADP translocator from R. prowazekiishare about 66% similarity (Kampfenkel et al, 1995;Williamson et al, 1989). However, even a high degree of similarity at the amino acid sequence level cannot be taken as definite proof that AATP1 indeed represents an ATP/ADP transtocator.…”

Section: Functional Expression Of the Cdna Encoding The Aatp1 Proteinmentioning

confidence: 99%

Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L.

et al. 1997

View full text Add to dashboard Cite

SummaryRecently, we have sequenced a cDNA clone from Arabidopsis thaliana L. encoding a novel putative ATP/ADP translocator (AATP1). Here, we demonstrate that the radioactively labeled AATP1 precursor protein, synthesized in vitro, is targeted to envelope membranes of isolated spinach chloroplasts. Antibodies raised against a synthetic peptide of AATP1 recognized a single polypeptide of about 62 kDa in chloroplast inner envelope preparations. The cDNA coding for the AATP1 protein was functionally expressed in Saccharomyces cerevisiae and Escherichia coil In both expression systems, increased rates of ATP transport were observed after reconstitution of the extracted protein into proteoliposomes. To our knowledge, this is the first report on the functional expression of an intrinsic plant membrane protein in E. coil To yield high rates of ATP transport, proteoliposomes had to be preloaded with ADP, indicating a counter-exchange mode of transport. Carboxyatractyloside did not substantially interfere with ATP transport into proteoliposomes containing the plastidic ATP/ADP translocator. An apparent KM for ATP of 28 llM was determined which is similar to values reported for isolated plastidso The data presented here strongly support the conclusion that AATP1 represents a novel eukaryotic adenylate carrier and that it is identical with the so far unknown plastidic ATP/ADP translocator.

show abstract

“…Radiolabeling of the cDNA, prehybridization, hybridization and washing was as outlined above. a protein of 589 amino acid residues which displays a significant similarity to the ATP/ADP translocator of the bacterium R. prowazekii [10] is shown in Fig. 1.…”

Section: Southern and Northern Blot Analysismentioning

confidence: 99%

Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants

et al. 1995

View full text Add to dashboard Cite

We have isolated an Arabidopsis thaliana cDNA encoding a highly hydrophobic membrane protein of 589 amino acids which contains 12 potential transmembrane helices and shows a high degree of similarity (43.5% identity, 66.2% similarity) to the ATP/ADP translocase of the Gram-negative bacterium Rickettsiaprowazekii, an obligate intracellular parasite responsible for the epidemic typhus. This rickettsial translocator resides in the cytoplasmic membrane and allows the bacterium to exploit the host cytoplasmic ATP pool. We hypothesize that the A. thaliana homolog of the R. prowazekii ATP/ADP translocase is the functional eukaryotic equivalent and resides in the plastid inner envelope membrane where it functions as an ATP importer.

show abstract

Nucleotide sequence of the Rickettsia prowazekii ATP/ADP translocase-encoding gene

Cited by 58 publications

References 44 publications

Charged amino-acid residues in transmembrane domains of the plastidic ATP/ADP transporter from Arabidopsis are important for transport efficiency, substrate specificity, and counter exchange properties

Charged amino-acid residues in transmembrane domains of the plastidic ATP/ADP transporter from Arabidopsis are important for transport efficiency, substrate specificity, and counter exchange properties

Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L.

Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants

Contact Info

Product

Resources

About