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:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The two major ribonuclease (EC 3.1.27.5) present in normal human urine have been highly purified and extensively characterized for their enzymatic, physical, chemical and structural properties. One of the enzymes, RNAase C, is a glycoprotein which exhibits a pH optimum of 8.5 with RNA as the substrate and preferentially degrades the synthetic homoribopolymer poly(C). This enzyme is resolved into multiple components by column electrofocusing. However, prior treatment with neuraminidase results in a single form of RNAase C with an isoelectric point of 10.4, indicating that the charge heterogeneity is the result of variability in sialic acid content. Amino acid composition and NH2- and COOH-terminal sequence analyses of RNAase C show that this enzyme is very similar to mammalian pancreatic RNAases; the data indicate a peptide chain of 126 amino acid residues and a 33% carbohydrate content. The second enzyme isolated from urine, termed RNAase U, is also a glycoprotein which has a pH optimum of 7.0 with RNA as substrate and is virtually inactive against poly(C). RNAase U lacks sialic acid and focuses as a single component with a highly basic isoelectric point of greater than pH 11.0. The NH2- and COOH-terminal sequences of RNAase U show little homology with the pancreatic RNAases. However, the amino acid composition of this enzyme indicates it is very similar to human spleen RNAase.
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PMID:Purification and properties of ribonucleases from human urine. 721 38

Isolated nuclei incubated with [14C]protein hydrolysate are shown to incorporate labelled amino acids into the acid-insoluble fraction. Purified chromatin and the complex of DNA with firmly bound proteins possess similar ability. The optimum pH of the reaction is 6.5-7.0, 2 mM MgCl2 stimulates incorporation, the temperature optimum is 37-40 degrees C. Chloramphenicol depresses incorporation by 70%, puromycin by 40%, cycloheximide does not affect the chromatin activity. Incorporation does not depend on the presence of ATP or GTP, and is substantially inhibited by deoxyribonuclease but not by ribonuclease treatment of chromatin or of the nuclei. Specific activity of firmly bound chromatin non-histone proteins is higher than that of labile bound ones; histones are not labelled. After pronase treatment of proteins radioactivity changes to an acid-soluble state. The molecular weight of isolated labelled polypeptides is about 6000 as shown by gel filtration and the analysis of NH2-terminal amino acids. Labelled polypeptides firmly bound to DNA consist of 7-10 amino acids. Specific activity of proteins firmly bound to DNA increases linearly with the time of incubation of chromatin with [14C]protein hydrolysate, the activity curve of labile bound non-histone proteins has a distinct sygmoid character. The polypeptide-synthesizing activity of rat liver chromatin increases between 9 h and 21 h after partial hepatectomy. Irradiation with 800 rads 30 min before the operation prevents activation of amino acid incorporation. From nine amino acids studied alanine, methionine, lysine, tyrosine and arginine are not incorporated in the system described. Glutamic acid is polymerized most effectively. Glutamine, asparagine and glycine are incorporated 7-8 times less. The data are given indicating that the incorporation is not random when an amino acid mixture is present. Preincubation of chromatin with NAD+ but not with its analogues increases the polypeptide-synthesizing activity of chromatin. The activation is prevented by thymidine and nicotinamide. Storage (18 h at 2-4 degrees C) brings about a complete loss of the polypeptide-synthesizing activity of chromatin. The ability of 'old' chromatin to incorporate amino acids can be restored by preincubating it with NAD+. Storage of chromatin in the presence of 5 mM adenosine 3',5'-monophosphate (cAMP) does not result in decrease of the polypeptide-synthesizing activity. It is assumed that poly-(ADP-ribose) is the energy source for amino acid activation in the system described.
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PMID:Polypeptide-synthesizing activity of eukaryotic chromatin. Properties, dependence on poly(ADP-ribose) and connection with the cell cycle. 737 37

To study the interaction and the role of the metal ion in the reaction catalyzed by Escherichia coli ribonuclease HI (E. coli RNase HI), substrate analogues containing a phosphorothioate linkage or 2'-modified nucleosides at the cleavage site were used. In the presence of Mg2+, Mn2+, Co2+, Zn2+, or Cd2+, the phosphorothioate linkage with the RP-configuration was cleaved, while the SP-isomer was not. Kinetic studies showed that Mn2+ and Cd2+ facilitated the cleavage of the phosphorothioate to only a small extent, which indicated the absence of an interaction between the metal ion and this phosphate residue. The interaction of the metal ion with the 2'-functional group was analyzed by Mg(2+)-titration experiments using the -OH, -NH2, and -F substrates. From Hill plots, it was found that the KMg values were almost the same. These results are evidence of an interaction between Mg2+ and the 2'-functional group by the formation of an outer-sphere complex with a water molecule. The Hill coefficient of 1.0 for the -OH substrate indicated that a single Mg2+ ion is required for the catalysis.
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PMID:Role of the Mg2+ ion in the Escherichia coli ribonuclease HI reaction. 770 24

Bovine seminal ribonuclease (BS-RNase) is a homolog of RNase A with special biological properties that include specific antitumor, aspermatogenic, and immuno-suppressive activities. Unlike RNase A, BS-RNase is a dimer cross-linked by disulfide bonds between Cys31 of one subunit and Cys32 of the other. At equilibrium, this dimer is a mixture of two distinct quaternary forms, M = M and M x M. The conversion of M = M to M x M entails the exchange of NH2-terminal alpha-helices between subunits. Here, the cytotoxic activities of purified M x M were shown to be greater than those of purified M = M, despite extensive equilibration of M = M and M x M during the time course of the assays. Replacing Cys31 or Cys32 with a serine residue did not compromise the enzymatic activity of dimeric BS-RNase, but reduced both the fraction of M x M at equilibrium and the cytotoxicity. We conclude that the M x M form is responsible for the special biological properties of BS-RNase. Since cytosolic ribonuclease inhibitor binds tightly to monomeric but not dimeric BS-RNase and only the M x M form can remain dimeric in the reducing environment of the cytosol, we propose that BS-RNase has evolved its M x M form to retain its lethal enzymatic activity in vivo.
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PMID:Structural basis for the biological activities of bovine seminal ribonuclease. 773 87

Fetal rat liver expresses a 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/Fru-2,6-Pase2) form that differs from the adult liver enzyme in the inhibition by phosphorylation by the adenosine 3',5'-cyclic monophosphate-dependent protein kinase and in the recognition by an antibody specific for the NH2-terminal domain of the adult liver enzyme. Northern blot analysis shows that fetal hepatocytes contain a species of mRNA that is 2.2 kb in size and that exhibits the maximal levels after delivery. PFK-2/Fru-2,6-Pase2 mRNA analysis using a sensitive ribonuclease protection assay reveals the presence of nearly similar amounts of adult liver-specific and skeletal muscle-specific mRNA in fetal liver and hepatocytes during the last days of gestation, as well as a 233-bp protected fragment present in fetal liver. These results were confirmed by polymerase chain reaction using specific oligonucleotide pairs. Primer extension of fetal liver cDNA suggests the presence of two initiation sites of transcription. Analysis of the adult liver PFK-2/Fru-2,6-Pase2 protein during the perinatal transition using a specific antibody shows a marked accumulation of this form immediately after birth.
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PMID:Multiple forms of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase are expressed in perinatal rat liver. 877 45

The evolutionarily conserved dolichol-P-dependent N-acetylglucosamine-1-P transferase gene, ALG7, functions by initiating the dolichol pathway of protein N-glycosylation. In yeast, ALG7 has a complex expression pattern and plays a critical role in diverse cellular functions, including proliferation and morphological response. In Chinese hamster ovary cells (CHO), ALG7 gives rise to three mRNAs of 1.5, 1.9 and 2.2 kb. We report results of RNA blotting assays, ribonuclease protection, PCR-amplification and sequencing of the CHO ALG7 transcripts 5' and 3' ends which suggest that the 1.5 and 1.9 kb transcripts are produced as a consequence of initiation at 2 distinct start sites, 350-379 bp apart. The transcriptional start site for the 1.5 kb mRNA is positioned between the first two in frame ATGs, while that of the 1.9 kb species is located upstream of these two in-frame ATGs. In order to test the translational competence of the 1.5 and 1.9 kb mRNAs, we constructed DNA templates specifying these transcripts and used them for in vitro transcription/translation. Our data show that the 1.9 kb mRNA served in the synthesis of 36 and 24 kDa species, as well as a low-abundance 32 kDa protein. The 1.5 kb transcript gave rise to a translation product of 32 kDa. The latter is synthesized in CHO cells and hamster submandibular glands. These results suggest the possibility that the 1.5 and 1.9 kb transcripts give rise to related protein isoforms with different lengths of their NH2-terminal regions.
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PMID:Characterization of multiple transcripts of the hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase suggests functionally complex expression. 956 46

Combinatorial peptide synthesis in combination with affinity selection and high-resolution ion mobility/time-of-flight mass spectrometry (IM/TOFMS) analysis has been used to investigate the binding of a series of 96 related eight-residue peptides (with the general sequence NH2-GX1X2FX3X4X5G-CO2H, where X1 = L, F, V, Y; X2 = N, F; X3 = E, V, T; X4 = V, L; X5 = V, L) to the ribonuclease S protein. A key advantage of this strategy is that the IM/ TOFMS approach allows the relative abundances of individual library components (including numerous sequence and structural isomers) to be characterized before and after screening. The relative binding interactions of different sequences are assessed by comparing IM/TOFMS data for those components that pass through the column (as well as those that bind) to data for the library prior to screening. The high-affinity sequences that are found in this study are compared with those selected from much larger combinatorial libraries. The results suggest that many expected sequences in the large libraries may be missing (e.g., due to issues such as failure of specific steps during the synthesis or differences in solubility). Comparison of the binding sequences obtained in these studies and those reported previously indicates that screening results from large libraries should be interpreted with caution.
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PMID:Assessment of purity and screening of peptide libraries by nested ion mobility-TOFMS: identification of RNase S-protein binders. 1121 41

In sequel to our preliminary observations with peptidomimetic opioid compounds, we have further investigated immunomodulatory activity of one peptidomimetic compound (Tyr-NH-CH2-CH2-O-Phe-NH2) with peripheral blood mononuclear cells (PBMCs) of healthy volunteers/tuberculosis patients. This peptidomimetic compound was evaluated for its effect on purified protein derivative (PPD) stimulated lymphocyte proliferation in vitro, production of Th1 and Th2 cytokines by ELISA and ribonuclease protection assay. Our study shows the immunosuppressive potential of above synthetic peptidomimetic compound. This compound inhibited PPD stimulated human lymphocyte proliferation and this inhibition was reversed by opioid receptor antagonist, naloxone. Its immunosuppressive effect was further demonstrated by inhibition of interleukin-9 (IL-9), IL-10 but failed to influence IL-2, IL-15 and interferon-y (IFN-gamma) in PPD stimulated human PBMCs.
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PMID:Inhibition of antigen specific lymphocyte proliferation and cytokine stimulation by peptidomimetic opioid compound. 1209 65

Pseudomonas aeruginosa DNA ligase D (PaeLigD) exemplifies a family of bacterial DNA end-joining proteins that consist of a ligase domain fused to a polymerase domain and a putative nuclease module. The LigD polymerase preferentially adds single ribonucleotides at blunt DNA ends and, as we show here, is also capable of adding up to 4 ribonucleotides to a DNA primer-template. We report that PaeLigD has an intrinsic ability to resect the short tract of 3'-ribonucleotides of a primer-template substrate to the point at which the primer strand has a single 3'-ribonucleotide remaining. The failure to digest beyond this point reflects a requirement for a 2'-OH group on the penultimate nucleoside of the primer strand. Replacing the 2'-OH by a 2'-F, 2'-NH2, 2'-OCH3, or 2'-H abolishes the resection reaction. The ribonucleotide resection activity resides within a 187-amino acid N-terminal nuclease domain and is the result of at least two component steps: (i) the 3'-terminal nucleoside is first removed to yield a primer strand with a ribonucleoside 3'-PO4 terminus, and (ii) the 3'-PO4 is hydrolyzed to a 3'-OH. The 3'-ribonuclease and 3'-phosphatase activities are both dependent on a divalent cation, specifically manganese. PaeLigD preferentially remodels the 3'-ends of a duplex primer-template substrate rather than a single strand of identical composition, and it prefers DNA primer strands containing a short 3'-ribonucleotide tract to an all-RNA primer. The nuclease domain of PaeLigD and its bacterial homologs has no apparent structural or mechanistic similarity to previously characterized nucleases. Thus, we surmise that it exemplifies a novel phosphoesterase family, defined in part by conserved residues Asp-50, Arg-52, and His-84, which are essential for the 3'-ribonuclease and 3'-phosphatase reactions.
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PMID:Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial non-homologous end-joining protein, DNA ligase D. 1589 97

Young calves have to deal with at least three major situations that require profound physiological and digestive adaptations: adaptation to extra-uterine life (up to the first postnatal week), maintenance at a pre-ruminant stage over a long period (3 to 5 months or more), and weaning. This paper reports results obtained on the development (growth and differentiation) of the gastrointestinal tract, and on digestive enzyme activities as well as some aspects of the regulation by gut regulatory peptides. In the newborn calf, the maturation of the small intestine depends on pregnancy duration (preterm vs. full term) and ingestion of colostrum from first milking. The function of gut enterocytes evolves along with the changes from fetal to adult enterocytes. The origin of dietary protein in pre-ruminant and weaning calves modifies SI morphology. Chymosin, elastase II and lactase are typical postnatal enzymes, whereas pepsin, ribonuclease and amylase become important especially following weaning. Nitrogen digestibility increases during the first month of life and is modified by replacement of skim milk powder with non-milk proteins. Milk formula supplementation with Nabutyrate increases pancreatic secretions and digestibility. The gastrointestinal tract development depends on gut regulatory peptides plasma and luminal concentrations. The response to exogenous peptides is in relation with their number and type of functional receptors and with the animal age. Experimental work with young ruminants is important not only for the species involved, but also for its implications to other mammalians.
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PMID:Gastrointestinal tract and digestion in the young ruminant: ontogenesis, adaptations, consequences and manipulations. 1999 80


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