Action of a Proline Analogue,
            <scp>l</scp>
            -Thiazolidine-4-Carboxylic Acid, in
            <i>Escherichia coli</i>

Unger, Leon; DeMoss, R. D.

doi:10.1128/jb.91.4.1556-1563.1966

Cited by 26 publications

(9 citation statements)

References 22 publications

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“…The antimetabolite activity of 4-thiazolidine carboxylate was probably due to feedback inhibition of the proline biosynthetic enzymes. This compound has been reported to be a feedback inhibitor in a cell-free system, and it was also proposed to be incorporated into E. coli protein (22), but those experiments were performed with a prototrophic strain. This latter result is illustrative of the problem in interpreting the effects of amino acid analogues under conditions where they must compete with an internal pool of the natural amino acid.…”

Section: Resultsmentioning

confidence: 99%

“…In a further attempt to block the transport process, we have extended these studies to four analogues of proline: 4-thiazolidine carboxylate, 4-allo-hydroxyproline (cis-hydroxyproline), azetidine-2-carboxylate, and 3, 4-dehydro-203 proline. With the exception of cis-hydroxyproline, all of these have been reported to inhibit growth of E. coli, and the inhibition was reversed by adding proline to the growth medium (5,6,22). These experiments were performed with strains prototrophic for proline, and it was not possible to determine whether inhibition was caused by a block in proline biosynthesis or by incorporation of the analogue in polypeptides.…”

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confidence: 99%

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Effects of Proline Analogues on the Formation of Alkaline Phosphatase in Escherichia coli

Morris

Schlesinger

1972

J Bacteriol

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Two of the four proline analogues tested for their effect on the formation and activity of Escherichia coli alkaline phosphatase were able to substitute for proline in protein synthesis in a proline auxotroph. One of these, 3, 4-dehydroproline, effectively replaced proline and led to formation of an active enzyme under conditions where no proline was present in the polypeptides. Substitution of azetidine-2-carboxylate for proline prevented active enzyme formation, producing instead altered monomeric forms of the alkaline phosphatase. These were detected with antibodies specific to denatured forms of the enzyme, and they were also characterized, together with cellular proteins, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alkaline phosphatase, as well as several other proteins, is localized exterior to the bacterial cell cytoplasm in the periplasmic space. In the presence of azetidine-2-carboxylate, a substantial number of these periplasmic proteins retain their specific site of localization, and the denatured subunits of alkaline phosphatase were only detected in the periplasmic fraction of the cell. Thus, secretion of these proteins does not appear to require a high degree of specificity in the native structure of the polypeptide chain. The analogues 4-allohydroxyproline and 4-thiazolidine carboxylate were unable to substitute for proline in protein synthesis but they inhibited growth of E. coli.An important stage in the formation of the alkaline phosphatase of Escherichia coli (EC 3.1.3.1.) is the transport of the protein from its site of synthesis in the cytoplasm to its site of function in the periplasm, a region of the bacterial cell exterior to the cytoplasmic membrane. From studies with several alkaline phosphatase-negative mutants that synthesized antigenically related forms of the enzyme, we had determined that the protein was probably transported in the form of the subunit prior to dimerization and activation by metal (15). These latter two additional reactions are essential for production of an active enzyme. Support for this model of transport of the subunit came from observations that E. coli spheroplasts that were able to make protein but unable to form active alkaline phosphatase secreted subunits of this protein into the spheroplast medium (14). Mechanisms for the transport of large polypeptides across bacterial membranes have not been described, but any system of transport must possess a high degree of specificity because only a small frac-tion of bacterial proteins are localized outside the cytoplasm. We have attempted to determine whether the specificity for alkaline phosphatase transport lies in the secondary or tertiary structure of the polypeptide chain. Because protein structure depends upon the specific amino acid sequence in the polypeptide, we altered the primary structure with analogues of amino acids that were able to substitute for the naturally occurring amino acid in protein synthesis. Previous experiments with two histidine analogues (1,2, 4-triazole-3-alanine and ...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Effects of Proline Analogues on the Formation of Alkaline Phosphatase in Escherichia coli

Morris

Schlesinger

1972

J Bacteriol

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“…As a further remarkable feature of N ‐formylation, we notice that pre‐translational formylation of peptides introduced in the translation machinery an amino acid with a secondary amine group [formerly named an ‘imino’ group (Unger and DeMoss, 1966)], a notable exception in the proteogenic amino acids, proline aside. This has considerable consequences in the chemical development of polypeptide synthesis, likely to control the overall speed of the process.…”

Section: The Formylation Of Methionine‐loaded Initiator Trna Its Rolmentioning

confidence: 99%

One‐carbon metabolism, folate, zinc and translation

Danchin

Sekowska

You

2020

Microbial Biotechnology

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The translation process, central to life, is tightly connected to the one-carbon (1-C) metabolism via a plethora of macromolecule modifications and specific effectors. Using manual genome annotations and putting together a variety of experimental studies, we explore here the possible reasons of this critical interaction, likely to have originated during the earliest steps of the birth of the first cells.Methionine, S-adenosylmethionine and tetrahydrofolate dominate this interaction. Yet, 1-C metabolism is unlikely to be a simple frozen accident of primaeval conditions. Reactive 1-C species (ROCS) are buffered by the translation machinery in a way tightly associated with the metabolism of iron-sulfur clusters, zinc and potassium availability, possibly coupling carbon metabolism to nitrogen metabolism. In this process, the highly modified position 34 of tRNA molecules plays a critical role. Overall, this metabolic integration may serve both as a protection against the deleterious formation of excess carbon under various growth transitions or environmental unbalanced conditions and as a regulator of zinc homeostasis, while regulating input of prosthetic groups into nascent proteins. This knowledge should be taken into account in metabolic engineering.

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“…(b) A number of separate laboratories have now reported the isolation of hydroxyprolyl-t-RNA and infer that t-RNA is the site for hydroxylation of proline (Coronado et al 1963;Manner & Gould, 1963;Coronado, Mardones, Celis & Allende, 1964;Jackson, Watkins & Winkler, 1964;Urivetsky, Frei & Meilman, 1965). It now seems beyond doubt that this complex occurs naturally but its relation to collagen biosynthesis has not been proved.…”

Section: Amino Acids Occasionally Encountered In Proteinsmentioning

confidence: 99%

Amino Acid Selection in Protein Biosynthesis

Peterson¹

1967

Biological Reviews

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Action of a Proline Analogue, l -Thiazolidine-4-Carboxylic Acid, in Escherichia coli

Cited by 26 publications

References 22 publications

Effects of Proline Analogues on the Formation of Alkaline Phosphatase in Escherichia coli

Effects of Proline Analogues on the Formation of Alkaline Phosphatase in Escherichia coli

One‐carbon metabolism, folate, zinc and translation

Amino Acid Selection in Protein Biosynthesis

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