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Biomedical subjects

S Nishimura

Publications and source records attributed to S Nishimura.

At least 919 records · Page 51Linked to original sources
PubMed1979

Under-modified Y base in a tRHAPhe isoacceptor observed in tumor cells.

A fluorescent wye (Ye) was isolated from tRHAPhe specific to Ehrlich ascites cells. The structure was determined to be alpha-amino-beta-hydroxy-4,9,-dihydro-4,6-dimethyl-9-oxo-1-H-imidazo(1,2-alpha)purine-7-butyric acid: namely the compound lacking methyl carboxyl and methyl groups and thus is an under-modified precursor of hydroxy-Y base present in normal liver tRNAPhe.

Animals↗
PubMed1979

Three-dimensional structure of hyper-modified nucleoside Q located in the wobbling position of tRNA.

The hyper-modified nucleoside Q (queuosine) is exclusively located in the wobbling position of anticodons of tRNATyr tRNAHis, tRNAAsn and tRNAAsp that recognise codons NAUC (ref. 1). Queuosine and its hexose-containing derivatives are widely distributed in microorganisms, animals and plants. We confirm here the chemical structure of queuosine as 7-(3, 4-trans-4, 5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine (Fig. 1). The unique structural features of Q are the unusual cyclopentenediol side chain and the 7-deazaguanine ring. Queuosine is one of the most complicated modified nucleosides found thus far.

Anticodon↗
PubMed1979

Specific fluorescent labeling of 7-(aminomethyl)-7-deazaguanosine located in the anticodon of tRNATyr isolated from E. coli mutant.

Under-modified E. coli tRNATyr that contains 7-(aminomethyl)-7-deazaguanosine in place of Q nucleoside can be chemically modified by dansyl chloride under neutral conditions. Fluorescent labelling specifically occurred only in the 7-(aminomethyl)-7-deazaguanine moiety. The modified tRNATyr was found to be active both in aminoacylation and in binding to ribosomes.

Anticodon↗
PubMed1979

Nucleotide sequence of starfish initiator tRNA.

The nucleotide sequence of starfish ovary initiator tRNA was determined to be pA-G-C-A-G-A-G-U-m1G-m2G-C-G-C-A-G-U-G-G-A-A-G-C-G-U-G-C-U-G-G-G-C-C-C-A-U-t6A-A-C-C-C-A-G-A-G-m7G-D-m5C-C-G-A-G-G-A-psi-C-G-m1A-A-A-C-C-U-C-G-C-U-C-U-G-C-U-A-C-C-AOH. The sequence was determined by a combination of the two different post-labeling techniques. Two-dimensional cellulose thin-layer chromatography was adopted for analysis of 5'-terminal nucleotides of tRNA fragments produced by formamide treatment. The nucleotide sequence of starfish initiator tRNA is very similar to that of mammalian cytoplasmic initiator tRNAs, but has seven different nucleotide residues and two modifications: residue 55 is psi instead of U, and residue 26 is unmodified G instead of m2G.

Amino Acyl-tRNA Synthetases↗
PubMed1979

1H NMR studies on the conformational characteristics of 2-thiopyrimidine nucleotides found in transfer RNAs.

The molecular conformations of naturally occurring 2-thiopyrimidine nucleosides (5-methylaminomethyl-2-thiouridine, 5-methoxycarbonylmethyl-2-thiouridine and 2-thiocytidine) and 5'-mononucleotides (5-methylaminomethyl-2-thiouridine 5'-monophosphate and 2-thiocytidine 5'-monophosphate) in 2H2O solution were elucidated by analyses of the proton NMR spin-coupling constant, nuclear Overhauser effect, and lanthanide-induced shifts and relaxation enhancements. As monomers, these nucleotides are almost exclusively in the 3E-gg-anti form, even in the absence of ordinary stabilizing factors of this form; i. e., base-stacking and base-pairing interactions with other nucleotide units. This inherent conformational rigidity of the 2-thiopyrimidine units probably contributes to stability of the conformation of tRNA.

Escherichia coli↗
PubMed1979

Isolation and characterization of a guanine insertion enzyme, a specific tRNA transglycosylase, from Escherichia coli.

A guanine insertion enzyme (tRNA transglycosylase) was purified to a homogeneous state from Escherichia coli B by ammonium sulfate fractionation and DEAE-cellulose, DEAE-Sephadex A-50, phosphocellulose, and Sephadex G-200 column chromatographies. The molecular weight of the enzyme, which appeared to be a single polypeptide, was 4.6 X 10(4) by sodium dodecyl sulfate gel electrophoresis. The enzyme catalyzes exchange of guanine with guanine located in the first position of the anticodon of tRNATyr, tRNAHis, tRNAAsn, and tRNAAsp, but unlike the enzymes isolated from rabbit reticulocytes and Ehrlich ascites tumor cells it does not catalyze the exchange of guanine with queuine (7-(3,4-trans-4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanine) present in these tRNAs. The pH optimum of the reaction was 7.0, and the pH1 value was 4.6 to 4.8. The reaction required Mg2+ ion. 7-Methylguanine inhibited guanine insertion, but the other purine analogues tested were not inhibitory and could not replace guanine.20

Base Sequence↗
PubMed1979

Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction.

The guanine insertion enzyme isolated from Escherichia coli (tRNA transglycosylase) catalyzed the incorporation of bases of Q (queuosine) precursors into E. coli undermodified tRNAAsn and tRNATyr. These bases of Q precursors were inserted in the first position of the anticodon of tRNASn and tRNATyr, replacing guanine originally located in that position. This is a novel type of post-transcriptional modification, inserting a modified base into the polynucleotide chain by cleavage of the N--C glycoside bond without breakage of the phosphodiester bond. One of the bases of Q precursors, 7-(aminomethyl)-7-deazaguanine, was found in the acid-soluble fraction of E. coli cells, supporting the conclusion that formation of Q, 7-(3,4-trans-4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine, in tRNA in vivo actually proceeds by the tRNA transglycosylase reaction.

Escherichia coli↗
PubMed1979

Fractionation of a mutagenic principle from broiled fish by high-pressure liquid chromatography.

A mutagenic principle present in the basic fraction of broiled sardines cooked in the ordinary way was fractionated by high-pressure liquid chromatography using a reversed-phase column. Results indicated that the major mutagenic principle is not identical with any of the mutagens previously isolated from amino acid pyrolysis products, and that a new, unidentified mutagen exists in broiled sardines.

Amino Acids↗
PubMed1979

Phosphoethanolamine as a growth factor of a mammary carcinoma cell line of rat.

We have identified phosphoethanolamine as the pituitary-derived growth-promoting material that specifically stimulates the rat mammary carcinoma cell line 64-24. We have been studying the growth characteristics of the 64-24 cell line, which was isolated from a highly hormone-dependent tumor and which retains in culture many characteristics of the original tumor. Previously, crude bovine pituitary extract was shown to contain a significant amount of growth-stimulating activity for these cells, and a growth factor from this extract was purified to homogeneity. This report describes the identification of the growth factor as phosphoethanolamine. Further, the biological activity of phosphoethanolamine was found to be virtually identical to that of the purified growth factor. A possible role of phosphoethanolamine in the growth of mammary tumor cells as well as of normal mammary epithelial cells and other tissues is discussed.

Animals↗