Literature DB >> 7802542

Anaerobic growth of Salmonella typhimurium on L(+)- and D(-)-tartrate involves an oxaloacetate decarboxylase Na+ pump.

G Woehlke, P Dimroth.   

Abstract

We show here that the Enterobacterium Salmonella typhimurium LT2 has the capacity to grow anaerobically on L(+)- or D(-)-tartrate as sole carbon and energy source. Growth on these substrates was Na(+)-dependent and involved the L(+)- or D(-)-tartrate-inducible expression of oxaloacetate decarboxylase. The induced decarboxylase was closely related to the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae as shown by the sensitivity towards avidin, the location in the cytoplasmic membrane, activation by Na+ ions, and Western blot analysis with antiserum raised against the K. pneumoniae oxaloacetate decarboxylase. Participation of an oxaloacetate decarboxylase Na+ pump in L(+)-tartrate degradation by S. typhimurium is in accord with results from DNA analyses. The deduced protein sequence of the open reading frame identified upstream of the recently sequenced oxaloacetate decarboxylase genes is clearly homologous with the beta-subunit of L-tartrate dehydratase from Escherichia coli. Southern blot analysis with S. typhimurium chromosomal DNA indicated the presence of probably more than one gene for oxaloacetate decarboxylase.

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Year:  1994        PMID: 7802542     DOI: 10.1007/bf00301843

Source DB:  PubMed          Journal:  Arch Microbiol        ISSN: 0302-8933            Impact factor:   2.552


  20 in total

1.  Appendix. Sequence of the beta-subunit of oxaloacetate decarboxylase from Klebsiella pneumoniae: a correction of the C-terminal part.

Authors:  G Woehlke; E Laussermair; E Schwarz; D Oesterhelt; H Reinke; K Beyreuther; P Dimroth
Journal:  J Biol Chem       Date:  1992-11-15       Impact factor: 5.157

2.  Characteristics of Tartrate-fermenting Species of Clostridium.

Authors:  J Tabachnick; R H Vaughn
Journal:  J Bacteriol       Date:  1948-10       Impact factor: 3.490

3.  Detection of specific sequences among DNA fragments separated by gel electrophoresis.

Authors:  E M Southern
Journal:  J Mol Biol       Date:  1975-11-05       Impact factor: 5.469

4.  Nucleotide sequence and functional properties of a sodium-dependent citrate transport system from Klebsiella pneumoniae.

Authors:  M E van der Rest; R M Siewe; T Abee; E Schwarz; D Oesterhelt; W N Konings
Journal:  J Biol Chem       Date:  1992-05-05       Impact factor: 5.157

5.  ATP formation associated with fumarate and nitrate reduction in growing cultures of Veillonella alcalescens.

Authors:  W de Vries; R M Rietveld-Struijk; A H Stouthamer
Journal:  Antonie Van Leeuwenhoek       Date:  1977       Impact factor: 2.271

6.  Isolation and characterization of oxaloacetate decarboxylase of Salmonella typhimurium, a sodium ion pump.

Authors:  K Wifling; P Dimroth
Journal:  Arch Microbiol       Date:  1989       Impact factor: 2.552

7.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

Authors:  H Schägger; G von Jagow
Journal:  Anal Biochem       Date:  1987-11-01       Impact factor: 3.365

8.  Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula.

Authors:  J B Huder; P Dimroth
Journal:  J Biol Chem       Date:  1993-11-25       Impact factor: 5.157

9.  Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium.

Authors:  G Woehlke; K Wifling; P Dimroth
Journal:  J Biol Chem       Date:  1992-11-15       Impact factor: 5.157

10.  Cloning and nucleotide sequence of the gene (citC) encoding a citrate carrier from several Salmonella serovars.

Authors:  N Ishiguro; H Izawa; M Shinagawa; T Shimamoto; T Tsuchiya
Journal:  J Biol Chem       Date:  1992-05-15       Impact factor: 5.157

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9.  Genomic diversity of citrate fermentation in Klebsiella pneumoniae.

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10.  Non-essential genes form the hubs of genome scale protein function and environmental gene expression networks in Salmonella enterica serovar Typhimurium.

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  10 in total

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