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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antibodies against purine nucleotides were obtained from rabbits immunized with conjugates of bovine serum albumine with AMP or GMP. The antibodies purified by affinity chromatography on nucleoside monophosphate-human serum albumine-Sepharose columns inhibited RNA synthesis on native T4 phage DNA by E. coli RNA polymerase. The inhibition of transcription was due mainly to inhibition of the initiation stage of RNA synthesis.
Mol Biol (Mosk)
PMID:[Inhibition of RNA synthesis in vitro by antibodies against mononucleotides]. 9 37

The effect of m7GMP release from m7GMP-containing mRNA cap sequence m7GpppG by the embryonic chick lens m7GpppN-pyrophosphatase activity on the synthesis of lens proteins was examined in a newly developed homologous translation system derived from 15-day embryonic chick lenses. The synthesis of total lens polypeptides and delta-crystallin polypeptides, the major translation product, was inhibited 84% and 88%, respectively, by 0.5 mM m7GpppG; m7GMP (0.5 mM) inhibited total synthesis by 63% but was 33% less inhibitory toward delta-crystallin synthesis; GpppG and GMP were not inhibitors, m7GpppG inhibited met-tRNAfmet incorporation into 80S initiation complexes.
Mol Biol Rep 1979 Feb 15
PMID:Differential synthesis of lens proteins in the presence of m7G(5')pppG and cleavage product m7GMP in an embryonic chick lens cell lysate. 22 May 21

In a previous report we have shown that insulin increases the phosphorylation of an endogenous protein of mol. wt. 16 000 daltons in sarcolemma membranes. In the present work we have demonstrated that phosphorylations of exogenous histones by the sarcolemma membranes are also increased by insulin. These results indicate that insulin activates a cyclic-AMP-independent protein kinase in sarcolemma membranes. The stimulatory effect of insulin on protein phosphorylations is increased by GTP and its analogue GMP-P(NH)P. The insulin effect was increased 3--4-fold by micromolar concentrations of GTP. The effect by the analogue GMP-P(NH)P was somewhat less. In the absence of insulin guanosine nucleotides had no effect on phosphorylation of the proteins. The results suggest that GTP is a modulator in the activation of a sarcolemma membrane protein kinase by insulin.
Mol Cell Endocrinol 1979 Oct
PMID:The effect of insulin and guanosine nucleotides on protein phosphorylations by sarcolemma membranes from skeletal muscle. 22 62

A large number of hormones and neurotransmitters activate adenylyl cyclase [ATP, pyrophosphate lyase (cyclizing; EC 4.6.1.1.)] catalyzing the formation of cAMP and PPi from ATP in the presence of Mg2+. The cAMP formed is in turn responsible for eliciting the physiological responses of these hormones and neurotransmitters. In addition to hormones and neurotransmitters, fluoride ion, cholera toxin and guanyl nucleotides (GTP and GTP analogs such as GTP gamma S and GMP-P(NH)P) also stimulate adenylyl cyclase activity (Perkins, 1974; Birnbaumer, 1977; Gill, 1977). It has become evident that hormonally-responsive adenylyl cyclase is a multi-component system consisting of at least 3 physically distinct units. The first is the hormone receptor containing a specific site for a given hormone. The second is the catalytic moiety (C component) of adenylyl cyclase bearing the site responsible for catalysis of the cyclizing reaction. The third is the guanyl nucleotide regulatory subunit (G component) which binds guanyl nucleotide. Recently, a GTPase activity has been found to be associated with the G component of adenylyl cyclase (Cassel and Selinger, 1976; Cassel et al., 1977a, b; Lambert et al., 1979). In this review we will present information on the regulation of hormonally-responsive adenylyl cyclases. This is not intended to be a comprehensive review of the literature. Rather, it represents our views on the current status of the regulation of cAMP formation.
Mol Cell Endocrinol 1979 Dec
PMID:Guanyl nucleotide regulation of hormonally-responsive adenylyl cyclases. 23 Jan 2

Columns containing ribosomes translating poly(U) covalently bound with cellulose (solid-phase translating system) were used to study translocation in ribosomes. It is shown that the passing of elongation factor G (EF-G) with the non-cleavable analog of GTP (GMP-PCP) through a column containing pre-translocated ribosomes results in the increase of competence for puromycin (i. e. to the transition of pre-translocated peptidyl-tRNA into the post-translocated state) just as in the case of the passing of EF-G with GTP. On the other hand, it is shown that the passing of EF-G with GMP-PCP through a column with pre-translocated ribosomes makes them capable of binding the next aminoacyl-tRNA (i. e. leads to the vacation of the ribosomal A-site). Thus, by means of the two independent tests it is shown that EF-G-promoted translocation in the ribosome can proceed without GTP hydrolysis. On the basis of the data obtained, a controlled step-wise elongation of polypeptide with the participation of EF-G without GTP cleavage has been carried out in the solid-phase column system of translation.
Mol Biol (Mosk)
PMID:[Translocation in ribosomes induced by elongation factor G without cleavage of GTP. Study using a solid phase translation system in columns]. 25 70

The two species of Elongation Factor Tu coded for by the tufA and tufB genes were synthesized in UV-irradiated E coli infected by transducing phages bearing the separate genes. Both proteins interact similarly with EFTs, GDP, and phe-tRNA. Although the phe-tRNA.EFTu.GMP.PNP complex containing the tufA gene product binds somewhat more tightly to ribosomes, both proteins promote the complete process of binding phe tRNA to ribosomes at similar rates.
Mol Gen Genet 1978 Feb 07
PMID:A comparison of the activities of the products of the two genes for elongation factor Tu. 34 85

ATP gamma-(p-azidoanilidate) (1) and ATP gamma-(p-azidobenzyl)-methylanilidate (2) were shown to be competitive inhibitors for ATP and amino acid in tRNA aminoacylation catalyzed by E. coli MRE-600 phenylalanyl-tRNA synthetase (E.C.6.1.1.20). Low concentration (10(-5)--10(-6) M) of either ATP, gamma-anilidate or GMP stimulates the aminoacylation of tRNA suggesting their interaction with some nucleotide binding sites of the enzyme other than catalytic ones. Covalent photobinding of (1) to the enzyme does not inhibit aminoacylation, nor does it prevent nucleotides from activating the enzyme. UV-irradiation of the synthetase in the presence of (2) results in complete inactivation of the enzyme which can be prevented by phenylalanine or phenylalanine-ATP to save 50% of the enzyme activity but not ATP and tRNA. The photobinding of (2) to the enzyme in the presence of phenylalanine and ATP removes the activation of the enzyme by nucleotides suggesting that both the catalytic and effector sites of the synthetase are blocked in the same manner by compound (2).
Mol Biol (Mosk)
PMID:[Influence of the structure of photoreactive ATP analogs on the affinity modification of phenylalanyl-tRNA synsthetase. Modification of the enzyme at two types of nucleotide sites]. 38 88

The kinetic of 1H leads to 3H exchange between water and C(8)H-groups of the guanylic residues in poly(G) . poly(C) and poly(dG) . poly(dC) was investigated within the temperature range from 30 to 90 degrees in 0.5 M NaCl (pH 7.2). It was shown that the exchange in freshly dissolved preparations at temperatures lower than 50 degrees proceeds faster than that in the case of GMP. According to the ylide mechanism of the exchange reaction the observed acceleration of the exchange is considered as a consequence of associates formation in poly(G) . poly(c) and poly(dG) . poly(dC) solutions at temperatures lower than 50 degrees. Associates are stabilized by intermolecular hydrogen bonds in which N(7) atoms of guanylic residues take part. The increase of the temperature is accompanied by gradual disappearance of the exchange acceleration. The retardation of exchange, which is characteristic of most non-associated double-stranded polynucleotides and nucleic acids is observed at the temperatures above 60 degrees. The retardation points to thermal destruction of the associates at temperatures higher than 50 degrees. The associates which are characterized by ordered structure including several "side by side" arranged double-stranded molecules were observed by electron microscopy. The addition of EDTA to solutions as well as the increase of temperature leads to destruction of the associates whereas the addition of Mg2+ makes the associates more stable.
Mol Biol (Mosk)
PMID:[Study of the intermolecular association of poly(G).poly(c) and poly(dG).poly(dC) in solutions by methods of 1H to 3H exchange and electron microscopy]. 54 80

A method is proposed for analysis of natural and chemically modified polynucleotides which consists in enzymatic conversion of the polymer or oligomer into nucleosides followed by cation-exchange chromotography on the microcolumns. By using the method developed it was shown that after treatment of the yeast tRNAVal and tRNAPhe with monoperphthalic acid N-oxides of adenosine and cytidine were formed. Poly (U, G) was not modified at a measurable extent whereas GMP was decomposed. In tRNAVal (yeast)the adenosines and cytosines of the anticodon loop and 3'-end are most reactive; it is the case for the C17 of the diHU-loop as well. These data are in agreement with the results obtained for tRNA modification with other reagents and for limited enzymatic hydrolysis of the tRNAVal. The limitations of the reaction of the monoperphthalate with nucleic acids are briefly discussed.
Mol Biol (Mosk)
PMID:[Modification of tRNA 1 Val from yeast with monoperphthalic acid]. 121 65

The crystal structure of a mutant ribonuclease T1 (Y45W) complexed with a non-cognizable ribonucleotide, 2'AMP, has been determined and refined to an R-factor of 0.159 using X-ray diffraction data at 1.7 A resolution. A specific complex of the enzyme with 2'GMP was also determined and refined to an R-factor of 0.173 at 1.9 A resolution. The adenine base of 2'AMP was found at a base-binding site that is far apart from the guanine recognition site, where the guanine base of 2'GMP binds. The binding of the adenine base is mediated by a single hydrogen bond and stacking interaction of the base with the imidazole ring of His92. The mode of stacking of the adenine base with His92 is similar to the stacking of the guanine base observed in complexes of ribonuclease T1 with guanylyl-2',5'-guanosine, reported by Koepke et al., and two guanosine bases, reported by Lenz et al., and in the complex of barnase with d(GpC), reported by Baudet & Janin. These observations suggest that the site is non-specific for base binding. The phosphate group of 2'AMP is tightly locked at the catalytic site with seven hydrogen bonds to the enzyme in a similar manner to that of 2'GMP. In addition, two hydrogen bonds are formed between the sugar moiety of 2'AMP and the enzyme. The 2'AMP molecule adopts the anti conformation of the glycosidic bond and C-3'-exo sugar pucker, whereas 2'GMP is in the syn conformation with C-3'-endo-C'-2'-exo pucker. The mutation enhances the binding of 2'GMP with conformational changes of the sugar ring and displacement of the phosphate group towards the interior of the catalytic site from the corresponding position in the wild-type enzyme complex. Comparison of two crystal structures obtained provides a solution to the problem that non-cognizable nucleotides exhibit unexpectedly strong binding to the enzyme, compared with high specificity in nucleolytic activity. The results indicate that the discrimination of the guanine base from the other nucleotide bases at the guanine recognition site is more effective than that estimated from nucleotide-binding experiments so far.
J Mol Biol 1992 Feb 20
PMID:Three-dimensional structure of a mutant ribonuclease T1 (Y45W) complexed with non-cognizable ribonucleotide, 2'AMP, and its comparison with a specific complex with 2'GMP. 131 85


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