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:3.1.30.1 (S1 nuclease)
3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This paper describes the use of Escherichia coli to isolate Bal31 deletion mutants and single-base substitution mutants that functionally define the promoter of the maize chloroplast beta-ATPase gene (atpB). Promoter function in E. coli and in a chloroplast in vitro transcription system was determined by S1 nuclease protection experiments using RNA products from each mutant. The results show that in vitro the chloroplast RNA polymerase responds to the promoter point mutations in a quantitatively similar fashion to the E. coli RNA polymerase. Deletion analysis demonstrates that sequences 5' of the -35 region are not necessary for chloroplast promoter function in vitro and that the presence of an adjacent promoter drastically decreases the transcriptional activity of the atpB promoter in E. coli.
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PMID:Mutational analysis of the maize chloroplast ATPase-beta subunit gene promoter: the isolation of promoter mutants in E. coli and their characterization in a chloroplast in vitro transcription system. 300 65

We have isolated a cDNA clone for the beta-subunit of HeLa cell Na,K-ATPase, containing a 2208-base-pair cDNA insert covering the whole coding region of the beta-subunit. Nucleotide sequence analysis revealed that the amino acid sequence of human Na,K-ATPase exhibited 61% homology with that of Torpedo counterpart (Noguchi et al. (1986) FEBS Lett. in press). A remarkable conservation in the nucleotide sequence of the 3' non-coding region was detected between the human and Torpedo cDNAs. RNA blot hybridization analysis revealed the presence of two mRNA species in HeLa cells. S1 nuclease mapping indicated that they were derived from utilization of two distinct polyadenylation signals in vivo. Total genomic Southern hybridization indicated the existence of only a few, possibly one set of gene encoding the Na,K-ATPase beta-subunit in the human genome.
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PMID:Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit. 300 98

Microinjection into an axon of an identified invertebrate neuron is shown to be a useful technique for analyzing the mechanisms of fast axonal transport. It permits direct assessment of the effect of agents that cannot permeate the plasma membrane on the translocation of material in the axon. The actin filament depolymerizer DNase I, when injected into the axon of the Aplysia neuron R2, caused a local block of fast transport of [3H]glycoprotein. Two agents that should interfere with the functioning of actin filaments without causing extensive depolymerization, tne N-ethylmaleimide-modified nuclease S1 fragment of myosin (injected) and dihydrocytochalasin B (applied externally). had no effect. Together these results suggest that actin plays a structural role in the axonal cytoskeleton rather than a role in transport force generation, the effect of DNase I being mediated by structural disordering of the axoplasm. Experiments were also done with inhibitors of dynein, the microtubule-associated ATPase. erythro-9-[3-(2-Hydroxynonyl)]adenine blocked transport but vanadate was ineffective.
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PMID:Microinjection into an identified axon to study the mechanism of fast axonal transport. 618 16

Subunit 9 of ATPase is known to be encoded in the oli1 gene of yeast mitochondrial DNA. The oli1 transcripts of wild type and of a cytoplasmic "petite" mutant have been analyzed by hybridization of mitochondrial RNA to various DNA fragments from the internal and flanking regions of the gene and by S1 nuclease mapping of the 5' and 3' ends. The results of such studies indicate that the ATPase gene is co-transcribed with the downstream serine tRNA gene. The oli1 message and tRNA are generated by post-transcriptional processing. Two of the nucleolytic processing steps are blocked in the cytoplasmic petite mutant, resulting in the accumulation of several different intermediate transcripts containing both genes. Processing of the 3' ends occurs near a common seven-nucleotide sequence (5'-ATTCTTA-3') also found in the 3' regions of other mitochondrial genes. This sequence is proposed to be part of a signal necessary for either termination of transcription or RNA processing.
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PMID:oli1 Transcripts in wild type and in a cytoplasmic "petite" mutant of yeast. 631 19

The yeast mitochondrial genes coding for cytochrome c oxidase subunit I ( COX1 ) and the ATPase subunits 8 and 6 are organized in one transcription unit. Precise mapping of RNA termini with S1 nuclease and primer extension analysis shows that the 3' end of the COX1 mRNA and the 5' end of the ATPase precursor RNA are juxtaposed within a conserved dodecamer sequence (5'- AAUAAUAUUCUU -3'). Sequence comparison reveals that this motif is present downstream of nearly all protein-encoding genes, including extragenic unassigned reading frames ( URFs ) and two URFs located within introns. Also the 3' terminus of an RNA species derived from the URF -containing intron of the large rRNA gene maps within such a dodecamer sequence. It is likely, therefore, that this motif serves as a processing point in the generation of mature mRNA. From a comparison of the various transcription units, we infer that RNAs that originate from an endonucleolytic cleavage at this sequence have stable 3' termini, while further processing of the 5' ends occurs. The efficiency of the initial cleavage varies between the different positions at which the motif is present.
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PMID:Processing of yeast mitochondrial messenger RNAs at a conserved dodecamer sequence. 632 91

The structural properties of cardiac isomyosins from several species were compared using native gel electrophoresis, analysis of proteolytic digests, analysis of monoclonal antibody reactivity to specific proteolytic fragments on electroblots and S1 nuclease mapping with cDNA probes. The structure of specific regions of the myosin molecule was analyzed by reacting monoclonal antibodies with chymotryptic peptides of myosin separated by two-dimensional electrophoresis. The pattern of fragments reactive with antibody CCM-52 (epitope in LMM) was identical in all types of V3 isomyosin examined, and different in each type of V1 isomyosin. Peptides reactive with RCM-79 (epitope in HMM) were different from those reactive with CCM-52 and were also significantly different in each type of myosin examined. Thus, HC-alpha is structurally similar in the LMM portion of the molecule in all animals examined, while in the HMM region there are significant structural differences. HC-alpha differs from HC-beta, with structural differences in both LMM and HMM. We have also shown that atrial myosin HC and ventricular HC-alpha in the rabbit are indistinguishable both by RIA and peptide mapping analysis. The same conclusion was derived after analysis of the myosin HC mRNA expressed in rabbit atria and ventricles. Using cDNA probes specific for the alpha and beta myosin HC mRNA, we could not distinguish between the atrial myosin mRNA and ventricular HC alpha (V1 isomyosin) mRNA by S1 nuclease mapping experiments. Classification of different cardiac myosins is largely based on their mobility on native gel electrophoresis, immunological cross-reactivity, and ATPase activities.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Classification and characterization of cardiac isomyosins. 653

Enhanced sodium reabsorption by the kidney has a significant role in the development of genetic hypertension. In the spontaneously hypertensive rat (SHR) model of genetic hypertension, the enhanced sodium reabsorption likely arises from abnormal hormonal regulation of tubular transport. Since hormonal signaling pathways are coupled frequently via GTP binding proteins, one explanation for hormonal abnormalities in SHR would be a defect in a GTP binding protein or proteins. Recent work has suggested that the regulation of Na+,K(+)-ATPase activity by cholera toxin-sensitive GTP binding proteins is abnormal in SHR. The purpose of the present studies was to clone the alpha S-subunit, which is the subunit ADP ribosylated by cholera toxin, of GS protein to determine whether it is abnormal in SHR. Reverse transcription-polymerase chain reaction was able to detect mRNA for alpha S in both Wistar-Kyoto (WKY) rats and SHR. Northern analysis indicated that equivalent amounts of alpha S mRNA were present in WKY rats and SHR. S1 nuclease analysis demonstrated that there was no difference in the amount of alpha S short and long forms between WKY rats and SHR. Subcloning and sequencing of polymerase chain reaction products from WKY rats and SHR indicated that the alpha S forms present in renal cortex were identical. ADP ribosylation studies with cholera toxin demonstrated the presence of equivalent amounts of alpha S protein in WKY rats and SHR. Taken together, these results suggest that the abnormal regulation of Na+,K(+)-ATPase activity by a cholera toxin-sensitive pathway in SHR does not arise from a defect in the alpha S subunit.
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PMID:Cloning of the alpha-subunit of GS protein from spontaneously hypertensive rats. 796 19

Genomic clones coding for the Artemia franciscana sarco(endo)plasmic reticulum Ca-ATPase have been isolated. The restriction map of the overlapping clones covers a region of 65 kilobases of DNA. Nucleotide sequence of mRNA coding regions shows that the gene is divided into 18 exons separated by 17 introns. Compared with the structure of the rabbit sarco(endo)plasmic reticulum Ca-ATPase 1 gene, 12 of the introns are in the same position, 8 introns present in the rabbit gene are absent from A. franciscana, 4 introns present in A. franciscana are not found in rabbit, and the position of 1 intron is shifted one base between both genes. Southern blot analysis strongly suggests that this is the only sarco(endo)plasmic reticulum Ca-ATPase gene present in A. franciscana. Primer extension and nuclease S1 protection experiments have shown the existence of two main regions of transcription initiation separated by 30 nucleotides. Transcription is initiated in both regions at two or three consecutive bases. A hexanucleotide that includes the initiation sites is repeated in both transcription initiation regions. The nucleotide sequence of the promoter region shows the existence of several putative regulatory sites, including some that are muscle-specific such as one CArG box, 3 MEF-2, and 8 putative binding sites for muscle transcription factors of the MyoD family.
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PMID:Structure of Artemia franciscana sarco/endoplasmic reticulum Ca-ATPase gene. 817 20

The expression of the sarcoplasmic reticulum (SR) Ca(2+)-ATPase gene and the SR Ca2+ pump function were investigated in thoracic aortas of 5- and 17-week-old normotensive Wistar-Kyoto (WKY) rats and spontaneously hypertensive rats (SHRs). The relative level of the two isoforms of SR Ca(2+)-ATPase mRNA expressed in the aorta (i.e., SERCA 2a and SERCA 2b) was determined by quantitative S1 nuclease protection analysis and normalized to the level of alpha-smooth muscle (alpha-Sm) actin mRNA. The level of alpha-Sm actin mRNA itself was normalized to the level of 18S ribosomal RNA using slot-blot hybridization assays. Total SR Ca2+ pump activity was estimated by measuring the rate of oxalate-supported Ca2+ uptake in homogenates. At 5 weeks, the amount of SERCA 2a and SERCA 2b mRNA, normalized to 18S ribosomal RNA, and the ratio of alpha-Sm actin mRNA to 18S RNA were identical in SHR and WKY rats. The Ca2+ pump activity was similar in the two strains of rats at 5 weeks. From 5 to 17 weeks, the amount of SERCA 2a mRNA increased in both strains while the level of SERCA 2b mRNA remained constant. The Ca2+ pump activity was unchanged in SHRs and tended to decrease in WKY rats. Accordingly, the change in the ratio of the SR Ca(2+)-ATPase mRNA isoforms does not appear to influence SR function. The level of alpha-Sm actin mRNA and SERCA 2a mRNA increased in parallel from 5 to 17 weeks in both strains.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Age-related changes in sarcoplasmic reticulum Ca(2+)-ATPase and alpha-smooth muscle actin gene expression in aortas of normotensive and spontaneously hypertensive rats. 841 87

The human ATP1AL1 gene belongs to the family of Na,K-ATPase and H,K-ATPase (X,K-ATPases) genes. It encodes a catalytic subunit of hitherto unknown human ouabain-sensitive H,K-ATPase that represents a novel third group of X,K-ATPases distinct from the known Na,K-ATPase and gastric H,K-ATPase. Cloning of the ATP1AL1 gene is described in this report. The exon-intron structure of ATP1AL1 was found to be very similar to that of related genes. It contains 23 exons and spans approximately 32 kb of genomic DNA. All ATP1AL1 exons and 12 of its 22 introns were entirely sequenced. A total of nine Alu repeats were identified in introns. The transcription initiation site was mapped 187 bp upstream of the ATG initiation codon by primer extension and S1 nuclease protection analyses of RNA from human skin and colon. Sequence analysis of the 5'-flanking region (1.48 kb) revealed numerous potential binding sites for transcription factors Sp1 and AP2 and one putative NF-kappa B binding site. The 0.85-kb region from position -484 (5'-flanking region) to position +369 (intron 1) meets the structural criteria of a CpG island. It is suggested that the ATP1AL1 gene contains two poly(A) addition sites that may function in a tissue-specific manner.
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PMID:Genomic organization of the human ATP1AL1 gene encoding a ouabain-sensitive H,K-ATPase. 883 94


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