ArticleThe EMBO journal1995
(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 44 citations in OpenAlex.
- Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.PLoS genetics · 2016Article
- Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Inactivation of the ketoreductase gilU gene of the gilvocarcin biosynthetic gene cluster yields new analogues with partly improved biological activity.Chembiochem : a European journal of chemical biology · 2009Article
- A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase.Journal of molecular biology · 2008Article
- Inhibitory effect of heterologous ribosome recycling factor on growth of Escherichia coli.Journal of bacteriology · 2000Article
- Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Reverse gyrase from the hyperthermophilic bacterium Thermotoga maritima: properties and gene structure.Journal of bacteriology · 1998Article
- A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall.The Journal of cell biology · 1997Article
- Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.Protein science : a publication of the Protein Society · 1996Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
To better understand the evolution of a key metabolic pathway, we have sequenced the trpCFBA gene cluster of the hyperthermophilic bacterium Thermotoga maritima. The genes were cloned by complementation in vivo of trp deletion strains of Escherichia coli. The new sequences, together with earlier findings, establish that the trp operon of T.maritima has the order trpE(G.D)CFBA, which might represent the ancestral organization of the tryptophan operon. Heterologous expression of the trp(G.D) and trpC genes in E.coli and N-terminal sequencing of their polypeptide products showed that their translation is initiated at the rate start codons TTG and ATC, respectively. Consequently, the N-terminus of the trp(G.D) fusion protein is 43 residues shorter than previously postulated. Amino acid composition and sequence analyses of the protein products of T.maritima trpC (indoleglycerol phosphate synthase), trpF (phosphoribosyl anthranilate isomerase) and trpA (alpha-subunit of tryptophan synthase) suggest that these thermostable (beta alpha)8-barrel proteins may be stabilized by additional salt bridges, compared with the mesostable forms. Another notable feature is the predicted lack of the N-terminal helix alpha 0 in the alpha-subunit of tryptophan synthase.
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