Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Na+, K(+)-ATPase alpha-subunit cDNA of the sea urchin, Hemicentrotus pulcherrimus, was obtained by twice screening prism and gastrula lambda gt10 cDNA libraries using an oligonucleotide probe derived from a mostly conserved region, FSBA (5'-p-(fluorosulfonyl)-benzoyladenosine) binding site of cation transport ATPases. The 5'-end of the non-coding region was determined by primer extension and the region was amplified by 5'-RACE method. The sea urchin alpha-subunit cDNA consists of 4401 nucleotides and encodes 1038 amino acid residues (MW, 114 kDa). The predicted primary structure, except N-terminal region, has similar degree of high homology to various metazoan Na+, K(+)-ATPase alpha-subunits. Alignment of amino acid sequence and a hydropathy profile also predicts eight putative transmembrane segments at least. The phylogenetic tree suspected from alignment of amino acid sequences of 21 species suggests that sea urchin and vertebrate Na+, K(+)-ATPase alpha-subunits seem to have evolved from a common origin, before vertebrate alpha-subunit divided into three isoforms.
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PMID:cDNA cloning of Na+, K(+)-ATPase alpha-subunit from embryos of the sea urchin, Hemicentrotus pulcherrimus. 910 40

The RT PCR approach was used to obtain the nucleotide sequence of the mRNA of a sarco/endoplasmic reticulum calcium transporting ATPase (SERCA) from the cross-striated (phasic) part of the adductor muscle of the deep sea scallop. Initially, degenerate primers based on consensus sequences among SERCAs and tryptic fragments of the scallop Ca-ATPase were used. The sequence was then extended using homologous primers and the 5' and 3' ends of the transcript determined by 5' and 3' RACE. The mRNA codes for a polypeptide chain 994 amino acid residues long (coded for by 2982 nucleotides) and has a 195 bp 5' untranslated region, with a 697 bp 3' untranslated region. The scallop enzyme shows strongest amino acid similarity to the SERCA enzyme of Loligo, followed by those of Drosophila and Artemia. It resembles the vertebrate SERCA3 in that it does not possess the phospholamban binding motif and so is unlikely to be regulated by protein kinase A mediated signals.
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PMID:Amino acid sequence of a Ca(2+)-transporting ATPase from the sarcoplasmic reticulum of the cross-striated part of the adductor muscle of the deep sea scallop: comparison to serca enzymes of other animals. 978 99

In the present study, we demonstrate that the rabbit cortical collecting duct cell line RCCT-28A possesses three distinct H-K-ATPase catalytic subunits (HKalpha). Intracellular measurements of RCCT-28A cells using the pH-sensitive dye 2', 7'-bis(2-carboxyethyl)-5(6)-carboxyfluorescein (BCECF) indicated that the mechanism accounting for recovery from an acid load exhibited both K+ dependence and sensitivity to Sch-28080 characteristic of H-K-ATPases. Recovery rates were 0.022 +/- 0.005 pH units/min in the presence of K+, 0.004 +/- 0.002 in the absence of K+, and 0.002 +/- 0.002 in the presence of Sch-28080. The mRNAs encoding the HKalpha1 subunit and the H-K-ATPase beta-subunit (HKbeta) were detected by RT-PCR. In addition, two HKalpha2 species were found by RT-PCR and 5' rapid amplification of cDNA ends (5'-RACE) in the rabbit renal cortex. One was homologous to HKalpha2 cDNAs generated from other species, and the second was novel. The latter, referred to as HKalpha2c, encoded an apparent 61-residue amino-terminal extension that bore no homology to reported sequences. Antipeptide antibodies were designed on the basis of this extension, and these antibodies recognized a protein of the appropriate mass in both rabbit renal tissue samples and RCCT-28A cells. Such findings constitute very strong evidence for expression of the HKalpha2c subunit in vivo. The results suggest that the rabbit kidney and RCCT-28A cells express at least three distinct H-K-ATPases.
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PMID:H-K-ATPase in the RCCT-28A rabbit cortical collecting duct cell line. 995 Sep 54

Vacuolar proton-translocating ATPases (V-ATPase) are multisubunit enzyme complexes located in the membranes of eukaryotic cells regulating cytoplasmic pH. So far, nothing is known about the genomic organization and chromosomal location of the various subunit genes in higher eukaryotes. Here we describe the isolation and analysis of a cDNA coding for the 54- and 56-kDa porcine V-ATPase subunit alpha and beta isoforms. We have determined the genomic structure of the V-ATPase subunit gene spanning at least 62 kb on Chromosome (Chr) 4q14-q16. It consists of 14 exons with sizes ranging from 54 bp to 346 bp, with a non-coding first exon and an alternatively spliced seventh exon leading to two isoforms. The 5' end of the V-ATPase cDNA was isolated by RACE-PCR. The V-ATPase alpha isoform mRNA, lacking the seventh exon, has an open reading frame of 1395 nucleotides encoding a hydrophilic protein of 465 amino acids with a calculated molecular mass of 54.2 kDa and a pI of 7.8, whereas the beta isoform has a length of 1449 nucleotides encoding a protein of 483 amino acids with a calculated molecular mass of 55.8 kDa. Amino acid and DNA sequence comparison revealed that the porcine V-ATPase subunit exhibits a significant homology to the VMA13 subunit of Saccharomyces cerevisiae V-ATPase complex and V-ATPase subunit of Caenorhabditis elegans.
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PMID:Molecular cloning and chromosomal assignment of the porcine 54 and 56 kDa vacuolar H(+)-ATPase subunit gene (V-ATPase). 1005 22

The abundance of Na,K-ATPase and its alpha and beta subunit mRNAs is upregulated in cardiac and other target tissue by thyroid hormone (T3). Multiple Na,K-ATPase mRNA beta 1 species encoding an identical beta 1 polypeptide are expressed in the heart. The different mRNA beta 1 species result from utilization of two transcription start-sites in the first exon and multiple (five) poly(A) signals in the terminal exon of the beta 1 gene. In the present study we identify the mRNA beta 1 species that are expressed in rat ventricular myocardium under basal conditions, and determine whether they are differentially regulated by T3. mRNA beta 1 species were identified by 3'-RACE followed by DNA sequencing, and by Northern blotting using probes derived from different regions of rat cDNA beta 1. Five mRNA beta 1 species are expressed in rat heart: mRNA beta 1 species that are initiated at the first transcription start-site and end at the first, second and fifth poly(A) sites (resulting in mRNAs of 1630, 1810, and 2780 nucleotides), and mRNA beta 1 species initiated at the second transcription start-site and ending at the second and fifth poly(A) sites (resulting in mRNAs of 1500 and 2490 nucleotides); in order of increasing length, the five mRNAs constitute 0.04, 0.15, 0.38, 0.11 and 0.32 of total mRNA beta 1 content. In hypothyroid rats (induced by addition of propyl-thiouracil to the drinking water for 3 weeks), total mRNA beta 1 content decreased to 0.18 euthyroid levels, which was associated with a disproportionate 7.5-fold decrease in the abundance of the longest transcript (P < 0.05); transcripts initiating at the first transcription start-site and ending at the second poly(A) signal in hypothyroid hearts were 0.26 euthyroid levels (P < 0.05). Hyperthyroidism induced by injection of normal rats with three doses of 100 micrograms T3/100 g body weight every 48 h resulted in an overall approximately 2-fold increase in mRNA beta 1 content with no change in the fractional contribution of any of the mRNA beta 1 species. The results indicate a complex heterogeneity in the expression of mRNA beta 1 in myocardium.
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PMID:Na,K-ATPase mRNA beta 1 expression in rat myocardium--effect of thyroid status. 1009 77

Highly purified membranes isolated from the Golgi complex of the scaly green flagellate Scherffelia dubia (Chlorophyta) were subjected to Triton X-114 two-phase partitioning. Proteins in the detergent phase were analyzed by 2D gel electrophoresis and a major protein of 66 kD (p66) was N-terminally sequenced. The complete cDNA sequence of p66 was obtained by 3' RACE-PCR and screening of a cDNA library of S. dubia with a PCR probe derived from the 3' RACE. Sequence analysis of the cDNA clone identified p66 as subunit A of V-ATPase. Other major proteins in the isolated Golgi complex were immunoreactive to heterologous antibodies raised against subunit B or the holoenzyme of V-ATPase. A polyclonal (anti-p66) antibody raised against a recombinant, bacterially expressed p66 fusion protein recognized p66 in the isolated Golgi complex in western blots and localized the antigen by immunogold electron microscopy mostly to the scale reticulum but also to the Golgi stack within the Golgi complex. Concanamycin A-sensitive (but bafilomycin A1-insensitive) ATPase activity was present in the isolated Golgi complex, and monensin at 0.5-1 microM reversibly inhibited flagellar regeneration and resulted in swelling of Golgi cisternae. It is concluded that a functional V-ATPase is a major protein of the Golgi complex in S. dubia and is presumably associated with sorting processes at the endocytotic/exocytotic boundary of the Golgi complex.
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PMID:V-ATPase is a major component of the Golgi complex in the scaly green flagellate Scherffelia dubia. 1057

DNA fragments homologous to members of the family of P-type ion-motive ATPases were identified in Trypanosoma cruzi by polymerase chain reaction (PCR) amplification. The sequence of one fragment, which closely resembled (87% identity) the tandemly linked proton pumps in Leishmania, was used to characterize the H(+)-ATPase genes in T. cruzi. The T. cruzi proton pump locus contains four tandemly repeated genes (TCH1-4) separated by 1.1 kb intergenic regions. The nucleotide sequence of one cloned gene of the tandem array contains a 2775 nt open reading frame encoding a predicted 101908-Da protein of 925 amino acids. The TCH genes are expressed as 3.8 and 4.9 kb polyadenylated transcripts in the epimastigote stage; expression of both transcripts is reduced in metacyclic trypomastigotes. Results of 5' and 3' RACE transcript mapping indicate that the 3.8 kb message is generated from within the tandemly repeated locus. The 3.8 kb TCH transcript has the T. cruzi mini-exon appended to a short (40 nt) 5' untranslated region (UTR) and has a 927 nt 3' UTR. The full peptide sequence of the T. cruzi proton pump is 80% identical to the Leishmania pump but lacks the extended carboxyl tail present in the Leishmania ATPase. An antibody that recognizes the 110-kDa Leishmania donovani proton pump cross-reacts with a 100-kDa protein in lysates of T. cruzi epimastigotes.
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PMID:The Trypanosoma cruzi genome contains ion motive ATPase genes which closely resemble Leishmania proton pumps. 1107 65

A cDNA encoding a Ca-ATPase homologue, designated SMA3, was isolated from an adult cDNA library of Schistosoma mansoni. The full-length cloned DNA contains a 3105-bp open reading frame that potentially encodes a 1035-amino-acid protein with a M(r) of 113,729 and a pl of 6.48. Homology searches for SMA3 reveal high sequence identity with a variety of Ca-ATPases from evolutionarily diverse organisms. SMA3 is predicted to contain 10 transmembrane regions typical of this protein family as well as other conserved domains, such as the phosphorylation site and FITC binding domain. The greatest sequence identity (40-50%) is found to those Ca-ATPases belonging to the secretory pathway subclass. Identification of the 5' end of the SMA3 cDNA by RACE analysis reveals the presence of a 36-base spliced leader RNA, suggesting that the SMA3 pre-mRNA is processed by trans-splicing. Northern analysis reveals a single dominant transcript of 5 kb in adult RNA preparations. Antibodies raised against an amino terminal peptide detect the protein in the adult tegument, suggesting that SMA3 functions to help control Ca homeostasis within the tegument and may play a role in signal transduction at the host parasite interface.
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PMID:Schistosoma mansoni: molecular characterization of a tegumental Ca-ATPase (SMA3). 1156 Apr 14

Using degenerate primers, followed by 3' and 5' RACE and "long" PCR, a continuous 4050-bp cDNA was obtained and sequenced from rainbow trout (Oncorhynchus mykiss) gill. The cDNA included an open reading frame encoding a deduced protein of 1088 amino acids. A BLAST search of the GenBank protein database demonstrated that the trout gene shared high sequence similarity with several vertebrate Na(+)/HCO(3)(-) cotransporters (NBCs) and in particular, NBC1. Protein alignment revealed that the trout NBC is >80% identical to vertebrate NBC1s and phylogenetic analysis provided additional evidence that the trout NBC is indeed a homolog of NBC1. Using the same degenerate primers, a partial cDNA (404 bp) for NBC was obtained from eel (Anguilla rostrata) kidney. Analysis of the tissue distribution of trout NBC, as determined by Northern blot analysis and real-time PCR, indicated high transcript levels in several absorptive/secretory epithelia including gill, kidney and intestine and significant levels in liver. NBC mRNA was undetectable in eel gill by real-time PCR. In trout, the levels of gill NBC1 mRNA were increased markedly during respiratory acidosis induced by exposure to hypercarbia; this response was accompanied by a transient increase in branchial V-type H(+)-ATPase mRNA levels. Assuming that the branchial NBC1 is localised to basolateral membranes of gill cells and operates in the influx mode (HCO(3)(-) and Na(+) entry into the cell), it would appear that in trout, the expression of branchial NBC1 is transcriptionally regulated to match the requirements of gill pHi regulation rather than to match trans-epithelial HCO(3)(-) efflux requirements for systemic acid-base balance. By analogy with mammalian systems, NBC1 in the kidney probably plays a role in the tubular reabsorption of both Na(+) and HCO(3)(-). During periods of respiratory acidosis, levels of renal NBC1 mRNA increased (after a transient reduction) in both trout and eel, presumably to increase HCO(3)(-) reabsorption. This strategy, when coupled with increased urinary acidification associated with increased vacuolar H(+)-ATPase activity, ensures that HCO(3)(-) levels accumulate in the body fluids to restore pH.
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PMID:Integrated responses of Na+/HCO3- cotransporters and V-type H+-ATPases in the fish gill and kidney during respiratory acidosis. 1472 54

The yvgW gene of Bacillus subtilis has been reported to encode a product which resembles CPx-type ATPase having a function related to Cd2+ and Zn2+ resistance through efflux of this metal. We recently showed that yvgW gene product is also important for sporulation in B. subtilis. The present study was focused on the functional characterization of yvgW in the sporulation process of B. subtilis. The analysis of yvgW expression showed that a significant expression took place during the late stage of sporulation (T5-T8). The deletion of spoIIAC and spoIIGB genes, encoding for sigmaF and sigmaE, respectively, resulted in the complete elimination of yvgW-lacZ expression while the deletion of the spoIIIG coding for sigmaG decreased the yvgW-lacZ expression to only 37% that of the wild type level. In contrast, the deletion of spoIVCB gene coding for sigmaK had no significant effects on the yvgW-lacZ expression. Transcription initiation site of yvgW during sporulation was determined by 5'-RACE-PCR, indicating that -10 and -35 sequences exhibited very good homology with the consensus sequences recognized by RNA polymerase containing sigmaE. Moreover, through the construction of yvgWDelta537-1351::spc, yvgW mutant cells were investigated for their spore properties, such as their resistance profiles against heat, chloroform and lysozyme, pointing out that spores of the mutant cells showed high sensitivity to heat and chloroform, but resistance to lysozyme. The level of dipicolinic acid was also significantly reduced to approximately 63% in yvgW spores as compared to wild type spores. Furthermore, the analyses of the nutrition-specific germination and outgrowth characteristics of the null mutant and the wild type cells revealed no defect in the initiation of yvgW spore germination but they returned to vegetative state more slowly than the wild type spores in minimal medium.
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PMID:Sporulation-specific expression of the yvgW (cadA) gene and the effect of blockage on spore properties in Bacillus subtilis. 1690 59


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