Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two modifications in the Sanger two dimensional electrophoretic procedure for RNA analysis are reported. One increases resolution on the primary fingerprint to the point that digests of large RNAs, of the size 1500-3000 nucleotides yield well resolved fingerprint patterns. The other is a novel endonucleolytic procedure that proves useful in determining sequences of the large oligonucleotides produced by T1 ribonuclease. These modifications have been used in determining the catalogs of oligomers produced by T1 ribonuclease digestion of 16S rRNAs from three related organisms, Bacillus subtilis, B.pumilus and B.stearothermophilus. The possible effects of adaptation to a thermophilic niche on ribosomal RNA primary structure and the phylogenetic relatedness of the two mesophilic Bacilli are discussed.
J Mol Evol 1976 Apr 09
PMID:A comparison of the 16S ribosomal RNAs from mesophilic and thermophilic bacilli: some modifications in the Sanger method for RNA sequencing. 81 56

Particular RNA fragments obtained by action of pancreatic ribonuclease on purified RNAs originating from species totally unrelated to Agrobacterium tumefaciens (Escherichia coli, rabbit, monkey) are capable of inducing the formation of transplantable tumorous tissue when introduced at wounded sites in inverted stems of Datura stramonium maintained under axenic conditions on a medium containing auxin and kinetin. Reovirus RNA and a small size RNA (5-6S) isolated from RNA bound RNA directed DNA polymerase from Escherichia coli also induced the appearance of tumorous tissues which grow on solid synthetic medium in the absence of auxin and kinetin.
Mol Biol Rep 1976 Jul
PMID:Particular small size RNA and RNA fragments from different origins as tumor inducing agents in Datura stramonium. 82 81

Exponential growing Tetrahymena pyriformis organisms were labelled with (3H) uridine or (3H) adenosine. The labelled RNA was extracted and isolated by affinity chromatography on poly-uridylic-acid sepharose and further analysed by means of sucrose gradient centrifugation and RNase digestion. Experimental evidence proved the existence of RNase resistant poly adenylic-acid fragments in the RNA of Tetrahymena cells. This poly adenylic-acid segment has a sedimentation rate of 4-5 S and would be localised in the 10-12S region of the RNA which is probably the m-RNA.
J Mol Evol 1976 Aug 03
PMID:Fractionation of RNA from tetahymena by affinity chromatography on poly-U-Sepharose. 82 41

Disulphide-rich proteins of widely differing functions were aligned with the aid of their half-cystinyl residues. This led to the grouping of ribonuclease, phospholipase A, lysozyme, snake venom toxins, bee and scorpion venom peptides, and the plant proteins potatoe carboxypeptidase inhibitor, ragweed pollen allergen, mistletoe toxins and pineapple sulfhydryl protease inhibitor into one super-family of proteins. Very few deletions/insertions were needed to effect alignment and probabilities were calculated for random occurrence of the matches that were found.
J Mol Evol 1977 Aug 05
PMID:Homology of functionally diverse proteins. 89 36

In terms of the mechanical model of molecules, a calculation has been carried out of possible positions and binding energies of 1-methyl uracyl in the contact region of the ribonuclease S active site. In the most preferential orientation, 1-methyl uracyl forms hydrogen bonds C(2)=O(uracyl)...H-N(Thr-45), N-H...Ogamma (Thr-45), C(4)=O... ...H-Ogamma (Ser-123). The base position found (atom coordinates are given) is in complete qualitative agreement with the position of the uracyl in UpcA bound to ribonuclease S as revealed by X-ray analysis. The influence studied of methyl substitution in positions 3 and 5 of the pyrimidine cycle on the base orientation within the protein field. It has been shown that the formation of hydrogen bonds with Thr-45 and Ser-123 is not prerequisite for productive fixation of the phosphoribosyl nucleotide moiety in the catalytic region of the enzyme active site.
Mol Biol (Mosk)
PMID:[A theoretical analysis of the binding of methyl derivatives of uracil at the contact portion of the active center of ribonuclease S]. 94 May 57

Polyribosomal messenger RNA from HeLa cells contain 3'-OH-terminal polyadenylate sequences approximately 133 nucleotides in length (weight average). When analyzed at the ribonucleoprotein level of organization these poly(A)-rich sequences are found to contain tightly bound proteins. These proteins remain associated with the poly(A)-rich RNA during affinity chromatography of RNase A and T1-digested polyribosomes on poly(U)-Sepharose in 0.5 M NaCl, and co-elute from the column with the RNA at 50% formamide. Controls establish that the co-purification of the proteins with poly(A) on poly(U)-Sepharose requires the molecular integrity of the poly(A). Polyacrylamide gel electrophoresis resolves the poly(A)-specific proteins into two components of 74,000 and 62,000 molecular weight. The larger protein is the same size as that previously reported to be associated with poly(A)-rich sequences in HeLa heterogeneous nuclear RNA (Kish, V.M., and Pederson, T. (1975), J. Mol. Biol. 95, 227-238). It is concluded that both HeLa nuclear and polyribosomal poly(A) sequences have a protein (62,000 molecular weight) associated with poly(A) appears to be confined only to messenger RNA.
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PMID:Poly (A)-rich ribonucleoprotein complexes from HeLa cell messenger RNA. 97 46

The quantitative changes of double-stranded RNA components of nuclear ribonucleo-protein particles containing pre-mRNA was investigated in the course of incubation of particles at 37 degrees C. The incubation of purified nuclear particles revealed the fragmentation of long double-stranded RNA sequences into shorter stretches. The presence of nuclear sap in the incubation mixture resulted in degradation of the double-stranded RNAs into acid soluble products. Autodegradation and/or ribonuclease treatment of nuclear RNP particles is accompanied by quantitative changes in the minor protein constituents of informofer.
Mol Biol Rep 1976 Nov
PMID:Autodegradation of pre-mRNA containing nuclear ribo-nucleoprotein particles. The effect of autodegradation on the double-stranded RNA sequences and on the protein composition of particles. 101 80

A procedure for the isolation and purification of a specific hybrid between rat 28S and 18S ribosomal RNA's and nucleolar DNA is described. The method employed includes the following steps: 1) isolation of the nucleolar DNA, 2) hybridization of [14C]rRNA with the nucleolar DNA, and 3) isolation and purification of the rRNA-DNA hybrid complex by chromatography on hydroxylapatite and centrifugation in a CsCl density gradient. In the isolated hybrid complex the RNA:DNA ratio is close to 1:1, and the degree of enrichment of the DNA by the rRNA cistrons is about 1500 times. The hybrid obtained has a sedimentation constant on the order of 20S, is resistant to the action of pancreatic RNase and RNase T1 and sheep brain DNase, and is characterized by high thermostability. Acording to the physicochemical tests used, the rRNA-DNA hybrid complex is a double-stranded poly-nucleotide with an ordered secondary structure.
Mol Biol (Mosk)
PMID:Isolation of a hybrid between rat ribosomal RNA and DNA. 102 44

After the annealing of pre-mRNA at high Cot values, up to 20% of the material becomes resistant to the action of ribonuclease. This has been attributed to the presence of self-complementary sequences (scRNA) in the pre-mRNA. The most important properties of scRNA, which was isolated in preparative amounts, have been studied. The approximate dimensions of the complementary segments are 45-50 nucleotides. Hybridization experiments have shown that scRNA is transcribed from repeated segments of the genome. It may be postulated that the rapidly hybridizing pre-mRNA fraction consists mainly of self-complementary sequences.
Mol Biol (Mosk)
PMID:Structure of nuclear pre-mRNA. VIII. Isolation and characterization of complementary sequences. 102 53

Variation of ribonuclease S structure is analysed with the potential energy being minimized by a computer. The function of potential energy contains the potentials of bond and angle distortions, torsional and non-valent interactions. It is shown that after 100 iterations the potential energy is decreased from the value of 6500 kcal/mole to--1012 kcal/mole, 92% of complete change of energy fitting the first ten iterations. The root mean square deviation (r. ms. d.) of final structure from the initial one is 0.232 A (0.206 A for the backbone and 0.257 A for side groups). The forbidden non-valent contacts are completely removed after minimization. R. ms. d. of the equilibrium value is decreased from 0.097 to 0.006 A for bond lengths; from 7.660 to 3.65 degrees for valence an-les and from 9.44 to 6.95 degrees for rotation angles around the peptide bonds. Distribution of tensions along the protein chain after minimization is considerably changed, the tensions decreasing in average by 100 times.
Mol Biol (Mosk)
PMID:[Theoretic analysis of conformation of proteins. I. Minimization of potential energy of ribonuclease S]. 105 89


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