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E L Tauson

Publications and source records attributed to E L Tauson.

6 recordsLinked to original sources
PubMed1988

[Lytic ability, in relation to gram-positive microorganisms, of a preparation isolated from a Pseudomonas lytica culture].

A lytic enzyme isolated from P. lytica was studied with respect to its effect on pathogenic grampositive and gramnegative organisms. All the grampositive organisms were lyzed by the enzyme to this or that extent. The cells of staphylococci were the most sensitive. The gramnegative organisms were resistant. It was suggested that the lytic enzyme could be used in preparing drugs for treating certain skin diseases caused by pathogenic staphylococci.

Bacteriolysis↗
PubMedDate not supplied

Identification of highly conserved hydrophobic amino acid motif in deduced amino acid sequence of Elymus sibiricus L. mitochondrial S13 ribosomal protein.

The nucleotide sequence of mitochondrial ribosomal protein rps13 gene from wild perennial grass Elymus sibiricus is presented. It was determined by the method of PCR amplification with specific oligonucleotide primers and the direct sequencing of the amplification product. The sequence of E. sibiricus mitochondrial gene for S13 predicts a hydrophobic ribosomal protein of 116 amino acids that shows strong similarity to those of wheat (99.7% identity) and maize (98%). The deduced amino acid sequence of S13 protein from E. sibiricus and homologous plant's (Zea mays, Daucus carota, Nicotiana tabacum, Marchantia polymorpha) and nonplant's (Escherichia coli) proteins shows the presence of hydrophobic amino acids' motif -L-X10-L-X10-M-X10-L-X10-L-. Slightly modified it can be found in many other ribosomal proteins. This conserved motif is presumed to be particularly important for association of the ribosomal S13 protein with other proteins in the small subunit of the mitochondrial ribosome.

Amino Acid Sequence↗
PubMedDate not supplied

[RNA editing in different genetic systems].

One of the significant amendments to the central dogma of the molecular biology was the discovery of the RNA editing process in different genetic systems. Whereas other forms of co- and posttranscriptional modifications of messenger RNA (mRNA) (capping, polyadenilation, splicing) retain the correspondence of the primary structure of exon and final transcript, RNA editing disturbs this correspondence changing the primary structure of mRNA after its transcription. The variants of RNA-editing mechanisms are various and include site-specific insertions and deletions of one or several nucleotides (insertion-deletion editing) as well as specific modifications of nucleosides such as C-->U and A-->I deamination or U-->C transamination (conversion editing). These mechanisms differ greatly in different genetic systems but they always result in synthesis of functionally valuable proteins from "incorrect" genes and, correspondingly, can play a significant role in regulation of their expression.

Animals↗
PubMedDate not supplied

[Editing of the mitochondrial cox3 transcript may yield a new site of protein-protein interactions in wild cereal Elymus sibiricus L].

With PCR, RT-PCR, and direct sequencing, complete nucleotide sequences were established for the Elymus sibiricus mitochondrial cytochrome c oxidase subunit 3 gene (cox3) and its cDNA. The cox3 transcript was shown to have 12 editing sites with changes affecting the amino acid sequence of the protein product. The editing of the primary cox3 transcript was found to change the position of a site of protein-protein interactions. The results demonstrate again the important role of mRNA editing in posttranscriptional regulation of the expression of plant mitochondrial genes.

Amino Acid Sequence↗
PubMedDate not supplied

[Specificity of hydrolysis of S. aureus 209P cell walls by a lytic preparation of Pseudomonas lytica].

Specificity of Staphylococcus aureus 209P cell wall hydrolysis by a lytic preparation isolated from the culture liquid filtrate of Pseudomonas lytica VKM V-1454D was studied by the dansylation method. The lytic preparation was found to contain the lytic proteinase lysing the cells of Gram-positive microorganisms. The enzyme hydrolysed the cell walls of S. aureus 209P releasing N-terminal glycine and alanine in amounts of 0.73 and 0.34 mumoles per 1 mumole of lysine, respectively, which indicated the cleavage of the bonds in the pentaglycine bridge and, apparently, of the bond between N-acetylmuramic acid.

Amino Acids↗