Literature DB >> 1766370

A Bacillus subtilis dipeptide transport system expressed early during sporulation.

C Mathiopoulos1, J P Mueller, F J Slack, C G Murphy, S Patankar, G Bukusoglu, A L Sonenshein.   

Abstract

Two previously identified Bacillus subtilis DNA segments, dciA and dciB, whose transcripts accumulate very rapidly after induction of sporulation, were found in the same 6.2 kb transcription unit, now known as the dciA operon. Analysis of the sequence of the dciA operon showed that its putative products are homologous to bacterial peptide transport systems. The product of the fifth gene, DciAE, is similar to peptide-binding proteins from Escherichia coli and Salmonella typhimurium (DppA and OppA) and B. subtilis (OppA). A null mutation in dciAE abolished the ability of a proline auxotroph to grow in a medium containing the dipeptide Pro-Gly as sole proline source, suggesting that the dciA operon encodes a dipeptide transport system.

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Year:  1991        PMID: 1766370     DOI: 10.1111/j.1365-2958.1991.tb00814.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  38 in total

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5.  New nucleotide sequence data on the EMBL File Server.

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Journal:  Nucleic Acids Res       Date:  1991-12-11       Impact factor: 16.971

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9.  Lyme disease-causing Borrelia species encode multiple lipoproteins homologous to peptide-binding proteins of ABC-type transporters.

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10.  Activation of the Bacillus subtilis hut operon at the onset of stationary growth phase in nutrient sporulation medium results primarily from the relief of amino acid repression of histidine transport.

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