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)

An altered form of the elongation factor 3 (EF-3) has been purified to near homogeneity from a thermolabile yeast mutant ts 13-06. The isolation procedure involved chromatography on DEAE-Sephadex, CM-Sepharose, and hydroxylapatite columns. The final purification of this protein was obtained by affinity chromatography on an ATP-Sepharose column. Because of the extreme lability of the mutant protein, the yield was very poor. Silver stain analysis of the sodium dodecyl sulfate electrophoretograms indicated that the affinity-purified protein was better than 90% pure. From the studies of the physical and biochemical properties, the following characteristics of the purified wild type and the mutant protein have been established. The two proteins were indistinguishable by their molecular weight, amino acid composition, and isoelectric point. Purified mutant EF-3 was rapidly inactivated between 37 and 39 degrees C. Under this condition, wild type EF-3 was completely stable. Ribosome-dependent GTPase and ATPase activities of the mutant EF-3 were heat sensitive; GTPase activity was more labile than the ATPase activity. Mutant EF-3, after exposure to a nonpermissive temperature, failed to stimulate binding of the ternary complex of EF-1 X GTP X aminoacyl-tRNA to ribosome. The wild type protein was fully active under this condition. Other biochemical and physical properties of these two proteins are under current investigation.
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PMID:Protein synthesis in yeast. Purification of elongation factor 3 from temperature-sensitive mutant 13-06 of the yeast Saccharomyces cerevisiae. 294 39

Evidence for the existence of factor(s) other than blood pressure responsible for modulation of myocardial hypertrophy accompanying hypertension is well documented. A factor that has been isolated from the myocardium of the spontaneously hypertensive rat and partially purified has been shown to stimulate protein synthesis in vitro. Three indexes of protein synthesis, namely incorporation of 3H-leucine into myocyte myosin, specific activity of the leucyl tRNA, and rate of protein synthesis, also were observed to significantly increase on exposure to this factor, which may play a key role in the modulation of myocardial hypertrophy that accompanies hypertension. Evidence has also been presented demonstrating the role of unknown factors that control the shift of myosin isozymes from V1 (a high-ATPase, high-contractile protein type) to V3 (a slow ATPase type myosin), and vice versa. This study demonstrates that the modulation of the myocardial mass can be controlled at different levels: first at an intrinsic intracellular level by the mechanism of a local growth factor, and then at the level of the contractile protein, the quality rather than quantity of which was found to be important. Both of these were observed to be modulated by factor(s) independent of blood pressure and myocardial mass. However, it remains to be determined what is responsible at the genetic level for transmitting the signal that selects what type of protein will be synthesized and whether there is a common pathway among all the controlling factors.
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PMID:Factors regulating myocardial hypertrophy in hypertension. 294 54

The nucleotide sequence (56,410 base-pairs) of the large single-copy region of chloroplast DNA from the liverwort Marchantia polymorpha has been determined. The sequence starts from one end (JLA) of the large single-copy region and encompasses genes for 21 tRNAs, six ATPase subunits (atpA, atpB, atpE, atpF, atpH and atpI), two photosystem I polypeptides (psaA and psaB), four photosystem II polypeptides (psbA, psbC, psbD and psbG), five ribosomal proteins (rps2, rps4, rps7, rps'12 and rps14), and three RNA polymerase subunits (rpoB, rpoC1 and rpoC2). In addition, we detected 18 open reading frames ranging from 29 to 2136 amino acid residues long, four of which share significant amino acid sequence homology to those of an Escherichia coli malK protein (designated mbpX), human mitochondrial ND2 (ndh2) and ND3 (ndh3) of a respiratory chain NADH dehydrogenase, or a bacterial antenna protein of a light-harvesting complex (lhcA). Sequence analysis suggests that four tRNA genes and six protein genes might be split by introns; they are trnG(UCC), trnK(UUU), trnL(UAA), trnV(UAC), atpF, ndh2, rpoC1, rps'12, ORF135 and ORF167. In the large single-copy region described here, the gene organization deduced is highly conserved with respect to that of higher plants, but an inversion of some 30,000 base-pairs flanked by trnL(CAA) and trnD(GUC) was seen between the liverwort and tobacco chloroplast genomes.
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PMID:Structure and organization of Marchantia polymorpha chloroplast genome. II. Gene organization of the large single copy region from rps'12 to atpB. 297 85

The sequence of the 16,019 nucleotide-pair mitochondrial DNA (mtDNA) molecule of Drosophila yakuba is presented. This molecule contains the genes for two rRNAs, 22 tRNAs, six identified proteins [cytochrome b, cytochrome c oxidase subunits I, II, and III (COI-III), and ATPase subunits 6 and 8] and seven presumptive proteins (URF1-6 and URF4L). Replication originates within a region of 1077 nucleotides that is 92.8% A + T and lacks any open reading frame larger than 123 nucleotides. An equivalent to the sequence found in all mammalian mtCDNAs that is associated with initiation of second-strand DNA synthesis is not present in D. yakuba mtDNA. Introns are absent from D. yakuba mitochondrial genes and there are few (0-31) intergenic nucleotides. The genes found in D. yakuba and mammalian mtDNAs are the same, but there are differences in their arrangement and in the relative proportions of the complementary strands of the molecule that serve as templates for transcription. Although the D. yakuba small and large mitochondrial rRNA genes are exceptionally low in G and C and are shorter than any other metazoan rRNA genes reported, they can be folded into secondary structures remarkably similar to the secondary structures proposed for mammalian mitochondrial rRNAs. D. yakuba mitochondrial tRNA genes, like their mammalian counterparts, are more variable in sequence than nonorganelle tRNAs. In mitochondrial protein genes ATG, ATT, ATA, and in one case (COI) ATAA appear to be used as translation initiation codons. The only termination codon found in these genes is TAA. In the D. yakuba mitochondrial genetic code, AGA, ATA, and TGA specify serine, isoleucine, and tryptophan, respectively. Fifty-nine types of sense condon are used in the D. yakuba mitochondrial protein genes, but 93.8% of all codons end in A or T. Codon-anticodon interactions may include both G-A and C-A pairing in the wobble position. Evidence is summarized that supports the hypothesis that A and T nucleotides are favored at all locations in the D. yakuba mtDNA molecule where these nucleotides are compatible with function.
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PMID:The mitochondrial DNA molecular of Drosophila yakuba: nucleotide sequence, gene organization, and genetic code. 300 25

We have previously reported the isolation and partial sequence analysis of a rice mitochondrial DNA fragment (6.9 kb) which contains a transferred copy of a chloroplast gene cluster coding for the large subunit of ribulose-1,5-bisphosphate carboxylase (rbcL), beta and epsilon subunits of ATPase (atpB and atpE), methionine tRNA (trnM) and valine tRNA (trnV). We have now completely sequenced this 6.9 kb fragment and found it to also contain a sequence homologous to the chloroplast gene coding for the ribosomal protein L2 (rpl2), beginning at a site 430 bp downstream from the termination codon of rbcL. In the chloroplast genome, two copies of rpl2 are located at distances of 20 kb and 40 kb, respectively, from rbcL. We have sequenced these two copies of rice chloroplast rpl2 and found their sequences to be identical. In addition, a 151 bp sequence located upstream of the chloroplast rpl2 coding region is also found in the 3' noncoding region of chloroplast rbcL and other as yet undefined locations in the rice chloroplast genome. Hybridization analysis revealed that this 151 bp repeat sequence identified in rice is also present in several copies in 11 other plant species we have examined. Findings from these studies suggest that the translocation of rpl2 to the rbcL gene cluster found in the rice mitochondrial genome might have occurred through homologous recombination between the 151 bp repeat sequence present in both rpl2 and rbcL.
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PMID:Rice mitochondrial genome contains a rearranged chloroplast gene cluster. 318 3

The location and nucleotide sequences of tobacco chloroplast genes for tRNAGlu(UUC), tRNATyr(GUA) and tRNAAsp(GUC) have been determined. These genes lie midway between the genes for alpha and beta/epsilon subunits of H+-ATPase on the large single-copy region of the chloroplast DNA. The gene organization is tRNAGlu - 59bp spacer - tRNATyr - 108bp spacer - tRNAAsp on the same DNA strand. Northern blot hybridization studies revealed that these three tRNA genes are cotranscribed. The transcription initiation site was localized at 24 bp upstream from the tRNAGlu coding region and its termination site at 90 bp downstream from the tRNAAsp coding region by S1 mapping. The tricistronic tRNA precursor is thus calculated to be 512 bases long. Its processing was also studied by S1 mapping.
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PMID:Structure and cotranscription of tobacco chloroplast genes for tRNAGlu(UUC), tRNATyr(GUA) and tRNAAsp(GUC). 400 Sep 34

Determination of sequences from the nine regions separating the large genes in the 19-kbp mitochondrial DNA from Torulopsis glabrata has led to the identification of 23 tRNA genes and to the recognition of two types of short repeated sequence implicated in mitochondrial genome expression. The two short repeated sequences are a nonanucleotide motif, 5'-TATAAGTAA-3' and a dodecanucleotide motif, 5'-TATAATATTCTT-3'. By RNA sequence determination it has been found that primary transcripts of the small and large rRNAs commence at the 3' penultimate adenine of the nonanucleotide sequence. This motif has also been found in the DNA sequence upstream from f-methionine, phenylalanine, leucine, tyrosine and glycine tRNAs, cytochrome oxidase subunit 2 and ATPase subunit 9. The dodecanucleotide sequence is found at least once in each of the nine regions between the large genes. Determination of the 3' ends of the small and large rRNAs has shown their location to be 8 and 23 nucleotides downstream from the dodecanucleotide sequence. This motif is thought to be involved in signalling processing of polycistronic transcripts. Such transcripts are invoked to account for the production of mRNAs for cytochrome b, cytochrome oxidase subunits 1 and 3, and the joint mRNA for ATPase subunits 8 and 6 genes that lack an adjacent upstream nonanucleotide transcription initiation signal sequence. Processing of polycistronic transcripts at tRNA sequences is also implicated in the formation of mature mRNAs. From the position of tRNA genes relative to the nonanucleotide motif it appears that clusters of these genes are co-transcribed with downstream sequences for cytochrome oxidase subunits 1 and 3.
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PMID:Location of transcriptional control signals and transfer RNA sequences in Torulopsis glabrata mitochondrial DNA. 404 Apr 62

1. Polyribosomes and ribosomal subunits from rat liver were adsorbed on a cellulosic ion-exchange adsorbent, freeze-dried and extracted with organic solvents. The activity of extracted particles in peptide elongation was tested in the presence of purified peptideelongation factors. 2. Chloroform-methanol mixture (2:1, v/v) extracted 1.87+/-0.15 pmol of cholesteryl 14-methylhexadecanoate/pmol of the smaller ribosomal subunit and 0.92+/-0.11 pmol/pmol of the larger subunit. 3. In the presence of transferase I, extracted polyribosomes and 40S subunits bound more phenylalanyl-tRNA than did control non-extracted particles. The same binding as in control mixtures was obtained with extracted particles supplemented with cholesteryl 14-methylhexadecanoate in quantities corresponding to those extracted. 4. The polymerization of phenylalanine was greatly decreased with extracted polyribosomes and subunits and addition of the cholesteryl ester could not fully restore the original activity. 5. Extraction significantly decreased the activity of the P site of peptidyl transferase and normal activity was recovered after the addition of the ester. The A site of peptidyl transferase in extracted polyribosomes showed an increased activity when compared with non-extracted polyribosomes. 6. Cholesteryl 14-methylhexadecanoate apparently affects the function of the ribosomal A site and peptidyl transferase site and probably also that of the guanosine triphosphatase site and P site. The presence of different amounts of the ester in polyribosomes may be one of the mechanisms modulating peptide elongation at the ribosomal level.
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PMID:Influence of cholesteryl 14-methylhexadecanoate on some ribosomal functions required for peptide elongation. 459 29

The GTP- and ATP-hydrolyzing activities of the rat liver 5S RNA-L5 (according to the proposed common nomenclature (1) protein complex designated as 5S RNP were stimulated by pig liver elongation factor 2 (EF-2) plus aminoacyl-tRNA, both of which were required for the stimulation. The stimulative effect of aminoacyl-tRNA on GTP hydrolysis by the complete system containing 5S RNP and EF-2 was dependent on the concentration of aminoacyl-tRNA. Aminoacyl-tRNA also stimulated ATP hydrolysis by the complete system but did not stimulate the ATP hydrolysis by 5S RNP alone or EF-2 alone. While deacylated tRNA stimulated the ATPase activity of the complete system, it had no effect on the GTPase activity. Preincubated tRNA lacking the 3'-terminal CCA moiety had little effect on the GTPase and ATPase activities of the complete system. Fusidic acid inhibited the GTPase and the ATPase activities of the complete system with and without aminoacyl-tRNA, although the extent of the inhibition was larger in the presence of aminoacyl-tRNA. These results suggest that 5S RNP may be a component of the GTPase center of rat liver 60S subunits.
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PMID:Stimulation by aminoacyl-tRNA of the GTPase and ATPase activities of rat liver 5S RNA protein particles in the presence of EF-2. 610 86

Previously, we have described an ATP-dependent recognition and binding of mRNA by eukaryotic initiation factors (eIF)-4A, eIF-4B, and eIF-4F (Grifo, J. A., Tahara, S. M., Leis, J. P., Morgan, M. A., Shatkin, A. J., and Merrick, W. C. (1982) J. Biol. Chem. 257, 5246-5252; Grifo, J. A., Tahara, S. M., Morgan, M. A., Shatkin, A. J., and Merrick, W. C. (1983) J. Biol. Chem. 258, 5804-5810). This finding was consistent with other studies which implicated eIF-4A and eIF-4B in binding mRNA to the 40 S ribosomal subunit, an ATP-requiring process. As part of ongoing studies of this step, and, in particular its ATP requirement, we have examined ATPase activity of various initiation factors. In this communication we describe an RNA-dependent ATP hydrolysis catalyzed by eIF-4A and eIF-4F. Although eIF-4B has little or no ATPase activity it can stimulate the RNA-dependent ATPase activity of either eIF-4A or eIF-4F. Similar to the ATP-dependent mRNA binding assay, the RNA-dependent ATPase activity is inhibited by the cap analogue m7GDP when globin mRNA is used as the activator. In addition, a variety of polynucleotides stimulate the ATPase activity of these factors including rRNA, tRNA, poly(U), and poly(A) but not poly(dA). Finally, an attempt has been made to discern whether phosphorylation or ATP hydrolysis is responsible for the ATP-stimulated binding of mRNA by eIF-4A and eIF-4B. We present evidence which is consistent with the interpretation that ATP hydrolysis and not protein phosphorylation correlates with ATP-stimulated binding of mRNA.
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PMID:RNA-stimulated ATPase activity of eukaryotic initiation factors. 614 16


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