Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.4 (ribonuclease)
 6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have studied the primary structure of 16S ribosomal RNA from Proteus vulgaris. The oligonucleotides containing methylated bases appeared to be the same as those of Escherichia coli, with one exception. We have also studied the base composition of the oligonucleotides obtained after T1 ribonuclease digestion of 16S RNA. On the basis both of their position on the fingerprint and of their pancreatic ribonuclease analyses, approximately 25 appeared to differ from those found in the E. coli T1 fingerprints. From the isolation of large fragments arising from the action of endogeneous endonucleases, we have concluded that the RNA sequences of both species are very similar. We have shown that the 5' and 3' extremities of 16S RNA are mostly conserved. It appears that the regions which are known to interact with ribosomal proteins in E. coli (particularly S8 and S15) are also less modified. It is noteworthy that the sequence modifications which have been observed are clustered and often correspond to regions of heterogeneity in E. coli 16S RNA.
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PMID:Comparative study of the 16S RNA's of Escherichia coli and Proteus vulgaris. 76 41

Yersinia pestis has been characterized in terms of fingerprints of digests (pancreatic and/or T1 ribonuclease) of its 16S and 5S ribosomal RNAs. These show clearly that Y. pestis is a member of the Enterobacteriaceae and suggest that within the Family it is most closely related to Serratia and/or Proteus.
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PMID:The phylogenetic status of Pasteurella pestis. 110 66

When RNA is annealed in solution with a sufficiently large excess of DNA, the kinetics of DNA-RNA hybridization are relatively simple. Methods are described for following the course of both DNA renaturation and DNA-RNA hybridization in this system. To explore the characteristics of the reaction a series of model systems was used. Each one utilized DNA (sheared to constant size) from a bacterium or bacteriophage and homologous cRNA, i.e. RNA synthesized in vitro on a template of the same DNA. Temperature optima were determined for the hybridization of Escherichia coli nucleic acids in 2xSSC and 3xSSC-50% formamide buffers, and of Proteus mirabilis nucleic acids in 2xSSC buffer. Rate-constants for DNA-RNA hybridization were measured by two methods. These gave somewhat different results, but in all cases the rate-constant of DNA-RNA hybridization was clearly less than that of DNA renaturation. Thus hybridization is a slower reaction than DNA renaturation. Nevertheless, in some cases, with a high concentration of DNA and a long annealing time, 90-95% of the added RNA became resistant to ribonuclease. Experiments are described which show that it is possible to deduce the analytical complexity of DNA with reasonable accuracy from its hybridization with complementary RNA. Similarly, it is possible to estimate the reiteration frequency of multiple DNA sequences (such as ribosomal DNA) from the hybridization of the total DNA with RNA complementary to the multiple sequences. The effect on the system of various DNA/RNA ratios from 100 to 1 is described.
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PMID:Molecular hybridization of ribonucleic acid with a large excess of deoxyribonucleic acid. 456 16

1. A comparison has been made between the ribonuclease activities of untreated ribosomes from Escherichia coli B and Pseudomonas fluorescens and the activities of ribosomes on to which ribosomal ribonuclease from E. coli B has been adsorbed. 2. The normal ribosomes from both species were stable in 5-10mm-Mg(2+) (I0.16) at pH6. The RNA in ribosomes from Ps. fluorescens was attacked by the adsorbed ribonuclease under these conditions, whereas the ribosomes from E. coli B were able to adsorb and inhibit this enzyme. 3. Inhibition was also observed with ribosomes from Aerobacter aerogenes, Proteus vulgaris and two other strains of E. coli. It was not observed in ribosomes from three species of Pseudomonas. 4. The inhibition depended on the integrity of the ribosomes and was not observed under conditions of low Mg(2+) concentration that cause irreversible degradation into more slowly sedimenting particles.
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PMID:The inhibition of ribosomal ribonuclease by bacterial ribosomes. 532 18

Phage X was isolated from sewage as plating on Escherichia coli or Salmonella typhimurium strains harbouring the incompatibility group X plasmid R6K. It also plated on a strain of Serratia marcescens carrying this plasmid. It failed to form plaques on Proteus mirabilis, P. morganii or Providencia alcalifaciens harbouring R6K, but did multiply on them. No phage increase occurred with homologous R- strains. Phage X also plated or registered an increase in titre on E. coli or S. typhimurium strains carrying various plasmids of incompatibility groups M, N, P-1, U or W as well as the unassigned plasmid R775. It adsorbed to pili determined by a group P-10 plasmid in a Pseudomonas aeruginosa strain but did not multiply on this organism. The phage was filamentous and curly, resistant to ribonuclease and diethyl ether and sensitive to chloroform. It adsorbed to the tips of pili.
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PMID:Phage X: a plasmid-dependent, broad host range, filamentous bacterial virus. 612 39

The percentage of bacteriocin-producing and phage-producing Klebsiella strains was as follows: K. pneumoniae-10%, K. ozaenae-7%, K. rhinoscleromatis-9%. The antimicrobial spectrum of the studied inducible particler was broad and was not limited by the frames of the genus and family. Bacteriocins and bacteriophages from Klebsiella were active to Klebsiella, Enterobacter, Escherichia, Shigella and Proteus representatives significant in medicine. Klebocins and Klebsiella phages exhibited antagonistic effects to phytopathogenic bacteria. Some strains of Erwinia and Pseudomonas were sensitive to phages or bacteriocins from Klebsiella. Bacteriocins protected corn and tomato seeds from contamination by erwinioses agents. All cultures of Agrobacterium, Corynebacterium, Micrococcus, Staphylococcus, Streptococcus were resistant to action of phages and klebocins. Bacteriocins from Klebsiella were assayed for their sensitivity to trypsin, chymotrypsin, lysozyme, ribonuclease, deoxyribonuclease. Action of klebocins was associated with a protein component. Proceeding from data of diffusion through the disc ultrafiltration membranes molecular weight of klebocins was in the range of 30,000 and 50,000 Da.
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PMID:[The antimicrobial spectrum of the action of bacteriocins and bacteriophages from Klebsiella strains]. 816 98