Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

DNA fragments isolated from Leishmania donovani ATPase genes were used to analyze the organization and expression of cation transporting ATPase genes in L. donovani, Leishmania tropica, Leishmania mexicana, Leishmania braziliensis, Trypanosoma brucei and Trypanosoma cruzi. The ATPase loci in all Leishmania species contained a tandem pair of ATPase genes arranged in head-to-tail orientation and separated by approximately 2 kb. No restriction site polymorphisms were detected in the internal portions of the Leishmania ATPase genes which contain domains conserved between the L. donovani and other eukaryotic plasma membrane ATPases. The ATPase locus of each of the four Leishmania species was mapped to a single small chromosome of approximately 750 kb. The ATPase locus of L. mexicana was differentially expressed. Promastigotes in exponential growth contained abundant transcripts from the upstream ATPase gene, while transcripts from the downstream gene were relatively scarce. Transcripts from the downstream ATPase gene increased in abundance in promastigotes allowed to reach the stationary phase of growth and were most abundant in amastigotes. The two trypanosome species were found to contain DNA fragments that hybridized strongly to the Leishmania ATPase gene.
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PMID:Conservation of cation-transporting ATPase genes in Leishmania. 182 63

Oligonucleotide primers were used to amplify DNA sequences from a plasma membrane cation transporting ATPase gene and a transcription factor IID (TFIID) gene from Pneumocystis carinii genomic DNA. The entire P. carinii ATPase gene was cloned from a genomic library by hybridization to the PCR-amplified DNA product. The nucleotide sequence of the gene contained a 2,799 base-pair open reading frame that encoded a 102,274 dalton protein composed of 933 amino acids. The P. carinii ATPase protein was 69-74% identical to four fungal proton pumps but less than 35% identical to protozoan and mammalian cation transporting ATPase genes or the Ca++ ATPases of Saccharomyces. The nucleotide sequence of a portion of the TFIID gene could be translated to produce a peptide of 53 amino acids in two regions of the sequence, interrupted by a 45 bp intron. The predicted TFIID amino acid sequence was identical to yeast TFIID genes in this region.
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PMID:PCR amplification of DNA sequences from the transcription factor IID and cation transporting ATPase genes in Pneumocystis carinii. 184 Jan 48

Southern blot screening of a genomic Helicobacter pylori library was employed to find a P type ATPase using a mixture of 16 DNA oligonucleotides coding for the DKTGT(I/L)T consensus sequence specific for the phosphorylation site of this family of ATPases. A positive clone, pRH439, was isolated and sequenced. The inserted 3.4-kb H. pylori DNA contained an intact open reading frame encoding a protein of 686 amino acids carrying the consensus sites for phosphorylation and ATP binding. The amino acid sequence exhibits a 25-30% identity with bacterial Cd2+ and Cu2+ ATPases. Genomic Southern blot analysis showed that this ATPase was present in all H. pylori strains examined, whereas it was not detectable in Campylobacter jejuni and other bacteria. The membrane topology of this ATPase was investigated using in vitro transcription/translation of fusion vectors to find signal anchor and/or stop transfer sequences. Eight regions of the H. pylori ATPase acted as signal anchor and/or stop transfer sequences and were ordered pairwise along the polypeptide chain placing the N and C-terminal amino acids in the cytoplasm. These transmembrane segments are contained between positions 73 and 92 (H1), 98 and 125 (H2), 128 and 148 (H3), 149 and 176 (H4), 309 and 327 (H5), 337 and 371 (H6), 637 and 658 (H7), and 659 and 685 (H8). The membrane domain of the ATPase, therefore, consists of at least four pairs of transmembrane segments with the phosphorylation site and ATP binding domain located in the large cytoplasmic loop between H6 and H7. The cytoplasmic domain contains several histidines and cysteines, perhaps indicative of divalent cation binding sites. There are several charged amino acids (3 Lys, 2 Glu, 2 Asp), predicted to be in the membrane domain mainly in H2, H3, and H4 and a Cys-Pro-Cys putative metal ion site in H6. The extracytoplasmic domain also has several charged amino acids (5 Glu, 1 Asp, 1 Lys, 1 Arg). It is likely that this novel protein is a heavy metal cation transporting ATPase and belongs to a family of P type ATPases containing eight transmembrane segments.
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PMID:Cloning and membrane topology of a P type ATPase from Helicobacter pylori. 855 Jun 1

In the fission yeast Schizosaccharomyces pombe, three P-type ATPases, namely Cta4p, Pmr1p, and Pmc1p, have been shown to be essential for Ca(2+) homeostasis and are required for specific cellular functions as well. Here, we show that the simultaneous deletion of pmc1(+) and SPAC29A4.19c, which encodes a putative P(5)-type ATPase, causes a hypersensitive growth to either high concentrations of Ca(2+) in a medium, or the antiarrhythmic drug amiodarone, which has been known to cause a disruption of Ca(2+) homeostasis. On the other hand, simultaneous deletion of pmr1(+) and SPAC29A4.19c causes a hypersensitive growth to Mn(2+) depletion in a medium. The green fluorescent protein-tagged SPAC29A4.19c protein reveals a typical localization pattern of the Golgi proteins, but the SPAC29A4.19c protein is not exchangeable in function with Pmr1p, which is required for Ca(2+)/Mn(2+) homeostasis in secretory pathways. These results suggest that the putative P(5)-type ATPase encoded by SPAC29A4.19c is essential for Ca(2+) and Mn(2+ )homeostasis in the absence of P(2)-type ATPases, Pmc1p or Pmr1p, respectively. According to the precedent nomenclature of calcium/cation transporting ATPase in fission yeast, SPAC29A4.19 was named cta5(+) in this study.
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PMID:Characterization of a fission yeast P(5)-type ATPase homologue that is essential for Ca(2+)/Mn(2+ )homeostasis in the absence of P(2)-type ATPases. 1916 88

P-type ion pumps are membrane transporters that have been classified into five subfamilies termed P1-P5. The ion transported by the P5-ATPases is not known. Five genes, ATP13A (ATPase type 13A) 1-ATP13A5, that belong to the P5-ATPase group have been identified in humans. Mutations of the human gene ATP13A2 underlie a form of PD (Parkinson's disease). Previous studies have suggested a relation between polyamines and P5B-ATPases. We have recently shown that the cytotoxicity induced by the polyamine analogue paraquat (1,1'-dimethyl-4,4'-bipyridinium), which is an environmental agent related to PD development, was increased in ATP13A2-expressing CHO (Chinese-hamster ovary) cells. In the present study we showed that ATP13A2-expressing CHO cells exhibit a 2-fold higher accumulation of spermidine. Increasing concentrations of spermidine reduced the viability of CHO cells stably expressing ATP13A2. The higher levels of spermidine attained by the ATP13A2-expressing CHO cells were correlated with an increase in the ATP-dependent spermidine uptake in an isolated subcellular fraction containing lysosomes and late endosomes. The results of the present study support the idea that the human P5B-ATPase ATP13A2 is involved in polyamine uptake.
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PMID:Parkinson's disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake. 2320 87