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evolution
the enzyme belongs to the RNase T1 family
evolution
the enzyme belongs to the RNase T1 family, comparison of the amino acid sequences, overview
evolution
the enzyme is a member of the RNase T1 family
evolution
the enzyme is a member of the RNase T1 family
malfunction
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deletion of gene rng leads to accumulation of 23S rRNA precursors in Escherichia coli
malfunction
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deletion of gene rng leads to accumulation of 23S rRNA precursors in Escherichia coli
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metabolism
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binase is involved in phosphate metabolism, low concentrations of extracellular inorganic phosphate induce the expression of phosphate regulon, Pho, genes, as well as the binase gene, binase expression is strongly dependent on a functional PhoP-PhoR two-component system
metabolism
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distinct roles of RNase E and RNase G in mRNA decay and tRNA processing, overview
physiological function
binase is a regulator of RNA-dependent processes of cell proliferation and apoptosis. Binase affects the total amount of intracellular RNA and the expression of proapoptotic and antiapoptotic mRNAs
physiological function
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barnase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin. Toxic extracellular RNases and antitoxic barstar build an analogous system
physiological function
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binase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin
physiological function
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RNase G is involved in maturation of the 5' end of the 23S rRNA processing the 5' region by cleaving the 77 extra nucleotides at the 5' end
physiological function
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RNase G is involved in the maturation of the 5' terminus of 16S rRNA, the processing of a few tRNAs, and the initiation of decay of a limited number of mRNAs but is not required for cell viability and cannot substitute for RNase E under normal physiological conditions
physiological function
the enzyme from Pleurotus ostreatus inhibits human tumor cell proliferation, e.g. of neuroblastoma cell lines IMR-32 and SK-N-SH and leukemia cell lines HL-60 and Jurkat. The enzyme causes a sub-G1-cell population formation in HL-60 cells, overview
physiological function
the enzyme inhibits human tumor cell line proliferation
physiological function
the enzyme is cytotoxic and inhibits the proliferation of human tumor cells, the enzyme is internalized into tumour cells
physiological function
the wild-type enzyme shows little inhibition of human tumor cell proliferation, but the mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N is inhibiting proliferation in human leukemia cell lines, HL-60 and Jurkat with IC50 values of 100 nM and 0.002 mM, respectively, mutant D31N/D38N/E92Q/D93N is inactive
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
RNase He1 shows little inhibition of human tumor cell proliferation
physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
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physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
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physiological function
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RNase G is involved in maturation of the 5' end of the 23S rRNA processing the 5' region by cleaving the 77 extra nucleotides at the 5' end
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physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
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physiological function
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ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
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additional information
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analysis of cumulative permeation and skin deposition of negatively charged RNAse T1 using porcine ear skin. RNAse T1 permeation is dependent upon current density,while skin deposition is not. RNAse T1 retains structural integrity and enzymatic function postiontophoresis. RNAse T1 appears to be bound to the epidermis alone
additional information
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comparison with barnase from Bacillus amyloliquefaciens, overview. Mutation in resD leads to a significant decrease in binase production, whereas mutation in spo0A causes its hyperproduction. Expression of binase is possible only in Spo0A-OFF cells
additional information
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comparison with binase from Bacillus pumilus, overview. Barnase expression is strictly dependent on activating Spo0A, the Spo0A protein is a multifunctional regulator that controls stress-related processes, such as sporulation, biofilm formation and cannibalism
additional information
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effects of water-water hydrogen bonding types upon the activity of the enzyme ribonuclease t1 through perturbation of the water hydrogen bonding distribution by using various salts, overview. Various salts differ in their ability to reduce the enzymatic activity of ribonuclease t1 correlated with the ability of each salt to promote high-angle hydrogen bonding in water. Increasing the population of high-angle hydrogen bonds among water molecules stabilizes the more compact, less active conformations of the enzyme
additional information
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neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles, encoding RNase E, even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants. Complementation of the growth defect associated with RNase E-deficient strains is dependent on the intracellular level of the Rng-219 and Rng-248 proteins
additional information
comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1
additional information
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comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1
additional information
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Trp59 may play an important role in folding as well as in modulating the geometry of the RNase T1 active site. Trp59-water pairs appear to preferentially participate in a hydrogen bond network incorporating polar amino acid moieties on the protein surface and bulk waters, providing the structural dynamic features of the connecting loop region in RNase T1, molecular dynamic simulations, overview
additional information
fluorescence spectroscopy of wild type (containing a single tryptophan, Trp59), 7-azatryptophan ((7-aza)Trp59-), and 2,7-diazatryptophan ((2,7-aza)Trp59-) substituted RNase T1 to probe the water environment of Trp59 near the connecting loop region gives insight of the structure-water network relationship
additional information
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fluorescence spectroscopy of wild type (containing a single tryptophan, Trp59), 7-azatryptophan ((7-aza)Trp59-), and 2,7-diazatryptophan ((2,7-aza)Trp59-) substituted RNase T1 to probe the water environment of Trp59 near the connecting loop region gives insight of the structure-water network relationship
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