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THIALYSINE UTILIZATION FOR PROTEIN-SYNTHESIS BY AN EXPONENTIALLY GROWING ESCHERICHIA-COLI CULTURE
No full textAspartokinase III repression and lysine analogs utilization for protein synthesis.
No full textThe extents of thialysine and selenalysine incorporation into cell proteins were compared in E. coli KL16 and in a mutant able to grow equally well in the presence or in the absence of both lysine analogs. The mutant differs from the parental strain in the repression of aspartokinase III (AKIII), the first enzyme of the lysine biosynthetic pathway. No analog incorporation into proteins was observed in mutant cells grown in the presence of either analog, whereas a marked analog incorporation was observed in the parental strain, where up to 17\% and 12\% of protein lysine can be substituted by thialysine and selenalysine respectively. In the parental strain grown in media containing either analog at different concentration the extent of analog incorporation into proteins is related to the extent of AKIII repression
Beta-selenaproline as competitive inhibitor of proline activation.
No full textBeta-Selenaproline, a proline analog having the beta-methylene group substituted by a selenium atom, has been tested in ATP-PPi exchange reaction catalyzed by either Escherichia coli or rat liver aminoacyl-tRNA synthetases. It has been shown that with both enzymatic systems beta-selenaproline does not give rise to ATP-PPi exchange, but specifically inhibits proline activation. The inhibition is of fully competitive type and the Ki values, lower than the Km values for proline, show that beta-selenaproline binds to the synthetases with high affinity. The inability to form the complex with AMP, taking into account also the behavior of gamma-selenaproline and other proline analogs, has been ascribed to the presence of the selenium atom in the beta-position
Transport systems for lysine, thialysine and selenalysine in E. coli KL16.
No full textTwo lysine transport systems have been identified in E. coli KL16. They differ in their affinity for lysine, one showing a KM of 0.36 microM and the other a KM of 4.7 microM. Different compounds with chemical similarities to lysine were tested for their capacity to interfere with lysine transport. Among these only thialysine and selenalysine competitively inhibit lysine transport. The inhibition is on both transport systems. Thialysine shows a KI of 4 microM for the low affinity system and a KI of 8 microM for the high affinity system. Selenalysine shows values of 6 microM and 12 microM respectively
Action of thiazolidine-2-carboxylic acid, a proline analog, on protein synthesizing systems
No full text[No abstract available
Recognition of aminoethylhomocysteine and aminopropylcysteine by aminoacid transport systems and aminoacyl tRNA synthetases.
No full textIn E. coli aminoethylhomocysteine (AEHC) and aminopropylcysteine (APC) do not affect intracellular lysine transport thus showing that they cannot bind the E. coli lysine transport systems. In CHO cells AEHC and APC inhibit lysine and arginine transport, AEHC more than APC, thus indicating that they can bind the cationic aminoacid transport system. They inhibit also leucine transport, APC more than AEHC. Some possible relationships between their structure and their effects on transport systems are considered. AEHC and APC are not activated by aminoacyl-tRNA synthetase preparations from bacterial and mammalian sources
Going Beyond Counting First Authors in Author Co-citation Analysis
Full text linkThe present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
Thialysine- and selenalysine-resistance in a E. coli mutant.
No full textA thialysine-resistant mutant of E. coli strain KL16 also shows a lower sensitivity to selenalysine, the lysine analog containing selenium. No difference between the mutant and the parental strain has been shown regarding the affinities of the transport systems and the lysyl-tRNA synthetase for selenalysine, thialysine and lysine as well as the inhibitory effects of these three aminoacids on the activity of the lysine biosynthetic pathway. A marked difference between the two strains has been evidenced in the AK III repression: in the mutant the repression by selenalysine, thialysine and lysine is much lower than in the parental strain
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